PubMed:11744633
Annnotations
Glycan-Motif
{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":174,"end":181},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":232,"end":239},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":323,"end":330},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":402,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T5","span":{"begin":733,"end":748},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T6","span":{"begin":941,"end":950},"obj":"https://glytoucan.org/Structures/Glycans/G40843KY"},{"id":"T7","span":{"begin":941,"end":950},"obj":"https://glytoucan.org/Structures/Glycans/G72548RZ"},{"id":"T8","span":{"begin":941,"end":950},"obj":"https://glytoucan.org/Structures/Glycans/G95090DW"},{"id":"T9","span":{"begin":1020,"end":1027},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T10","span":{"begin":1095,"end":1110},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
GlyCosmos6-Glycan-Motif-Image
{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":174,"end":181},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":232,"end":239},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":323,"end":330},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":402,"end":417},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":733,"end":748},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":941,"end":950},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":1020,"end":1027},"obj":"Glycan_Motif"},{"id":"T10","span":{"begin":1095,"end":1110},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G95090DW"},{"id":"A7","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G72548RZ"},{"id":"A8","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G40843KY"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A10","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
GlyCosmos6-Glycan-Motif-Structure
{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":174,"end":181},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":232,"end":239},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":323,"end":330},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":402,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T5","span":{"begin":733,"end":748},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T6","span":{"begin":941,"end":950},"obj":"https://glytoucan.org/Structures/Glycans/G40843KY"},{"id":"T7","span":{"begin":941,"end":950},"obj":"https://glytoucan.org/Structures/Glycans/G72548RZ"},{"id":"T8","span":{"begin":941,"end":950},"obj":"https://glytoucan.org/Structures/Glycans/G95090DW"},{"id":"T9","span":{"begin":1020,"end":1027},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T10","span":{"begin":1095,"end":1110},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
GlycoBiology-FMA
{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":40,"end":48},"obj":"FMAID:165243"},{"id":"_T2","span":{"begin":40,"end":48},"obj":"FMAID:61795"},{"id":"_T3","span":{"begin":69,"end":81},"obj":"FMAID:82737"},{"id":"_T4","span":{"begin":69,"end":81},"obj":"FMAID:197276"},{"id":"_T5","span":{"begin":113,"end":125},"obj":"FMAID:197276"},{"id":"_T6","span":{"begin":113,"end":125},"obj":"FMAID:82737"},{"id":"_T7","span":{"begin":149,"end":159},"obj":"FMAID:167265"},{"id":"_T8","span":{"begin":149,"end":159},"obj":"FMAID:167268"},{"id":"_T9","span":{"begin":149,"end":159},"obj":"FMAID:167267"},{"id":"_T10","span":{"begin":149,"end":159},"obj":"FMAID:62932"},{"id":"_T11","span":{"begin":149,"end":159},"obj":"FMAID:62933"},{"id":"_T12","span":{"begin":149,"end":159},"obj":"FMAID:62931"},{"id":"_T13","span":{"begin":151,"end":159},"obj":"FMAID:165243"},{"id":"_T14","span":{"begin":151,"end":159},"obj":"FMAID:61795"},{"id":"_T15","span":{"begin":168,"end":173},"obj":"FMAID:167330"},{"id":"_T16","span":{"begin":174,"end":181},"obj":"FMAID:82801"},{"id":"_T17","span":{"begin":174,"end":181},"obj":"FMAID:196796"},{"id":"_T18","span":{"begin":190,"end":197},"obj":"FMAID:165447"},{"id":"_T19","span":{"begin":190,"end":197},"obj":"FMAID:67257"},{"id":"_T20","span":{"begin":223,"end":231},"obj":"FMAID:61795"},{"id":"_T21","span":{"begin":223,"end":231},"obj":"FMAID:165243"},{"id":"_T22","span":{"begin":232,"end":239},"obj":"FMAID:196796"},{"id":"_T23","span":{"begin":232,"end":239},"obj":"FMAID:82801"},{"id":"_T24","span":{"begin":248,"end":255},"obj":"FMAID:165447"},{"id":"_T25","span":{"begin":248,"end":255},"obj":"FMAID:67257"},{"id":"_T26","span":{"begin":307,"end":317},"obj":"FMAID:167268"},{"id":"_T27","span":{"begin":307,"end":317},"obj":"FMAID:62933"},{"id":"_T28","span":{"begin":307,"end":317},"obj":"FMAID:167267"},{"id":"_T29","span":{"begin":307,"end":317},"obj":"FMAID:167265"},{"id":"_T30","span":{"begin":307,"end":317},"obj":"FMAID:62932"},{"id":"_T31","span":{"begin":307,"end":317},"obj":"FMAID:62931"},{"id":"_T32","span":{"begin":309,"end":317},"obj":"FMAID:165243"},{"id":"_T33","span":{"begin":309,"end":317},"obj":"FMAID:61795"},{"id":"_T34","span":{"begin":323,"end":330},"obj":"FMAID:82801"},{"id":"_T35","span":{"begin":323,"end":330},"obj":"FMAID:196796"},{"id":"_T36","span":{"begin":339,"end":346},"obj":"FMAID:67257"},{"id":"_T37","span":{"begin":339,"end":346},"obj":"FMAID:165447"},{"id":"_T38","span":{"begin":386,"end":394},"obj":"FMAID:165243"},{"id":"_T39","span":{"begin":386,"end":394},"obj":"FMAID:61795"},{"id":"_T40","span":{"begin":537,"end":547},"obj":"FMAID:196728"},{"id":"_T41","span":{"begin":537,"end":547},"obj":"FMAID:82739"},{"id":"_T42","span":{"begin":674,"end":684},"obj":"FMAID:62933"},{"id":"_T43","span":{"begin":674,"end":684},"obj":"FMAID:167268"},{"id":"_T44","span":{"begin":674,"end":684},"obj":"FMAID:62931"},{"id":"_T45","span":{"begin":674,"end":684},"obj":"FMAID:62932"},{"id":"_T46","span":{"begin":674,"end":684},"obj":"FMAID:167267"},{"id":"_T47","span":{"begin":674,"end":684},"obj":"FMAID:167265"},{"id":"_T48","span":{"begin":676,"end":684},"obj":"FMAID:165243"},{"id":"_T49","span":{"begin":676,"end":684},"obj":"FMAID:61795"},{"id":"_T50","span":{"begin":702,"end":710},"obj":"FMAID:61795"},{"id":"_T51","span":{"begin":702,"end":710},"obj":"FMAID:165243"},{"id":"_T52","span":{"begin":854,"end":864},"obj":"FMAID:167268"},{"id":"_T53","span":{"begin":854,"end":864},"obj":"FMAID:62932"},{"id":"_T54","span":{"begin":854,"end":864},"obj":"FMAID:167265"},{"id":"_T55","span":{"begin":854,"end":864},"obj":"FMAID:62931"},{"id":"_T56","span":{"begin":854,"end":864},"obj":"FMAID:62933"},{"id":"_T57","span":{"begin":854,"end":864},"obj":"FMAID:167267"},{"id":"_T58","span":{"begin":856,"end":864},"obj":"FMAID:165243"},{"id":"_T59","span":{"begin":856,"end":864},"obj":"FMAID:61795"},{"id":"_T60","span":{"begin":897,"end":905},"obj":"FMAID:61795"},{"id":"_T61","span":{"begin":897,"end":905},"obj":"FMAID:165243"},{"id":"_T62","span":{"begin":971,"end":982},"obj":"FMAID:196773"},{"id":"_T63","span":{"begin":971,"end":982},"obj":"FMAID:82780"},{"id":"_T64","span":{"begin":1011,"end":1019},"obj":"FMAID:165243"},{"id":"_T65","span":{"begin":1011,"end":1019},"obj":"FMAID:61795"},{"id":"_T66","span":{"begin":1020,"end":1027},"obj":"FMAID:196796"},{"id":"_T67","span":{"begin":1020,"end":1027},"obj":"FMAID:82801"},{"id":"_T68","span":{"begin":1036,"end":1043},"obj":"FMAID:67257"},{"id":"_T69","span":{"begin":1036,"end":1043},"obj":"FMAID:165447"},{"id":"_T70","span":{"begin":1207,"end":1219},"obj":"FMAID:82737"},{"id":"_T71","span":{"begin":1207,"end":1219},"obj":"FMAID:197276"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
uniprot-human
{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":138,"end":150},"obj":"http://www.uniprot.org/uniprot/Q9NQX3"},{"id":"T2","span":{"begin":149,"end":159},"obj":"http://www.uniprot.org/uniprot/P16581"},{"id":"T3","span":{"begin":307,"end":317},"obj":"http://www.uniprot.org/uniprot/P16581"},{"id":"T4","span":{"begin":674,"end":684},"obj":"http://www.uniprot.org/uniprot/P16581"},{"id":"T5","span":{"begin":854,"end":864},"obj":"http://www.uniprot.org/uniprot/P16581"},{"id":"T6","span":{"begin":469,"end":483},"obj":"http://www.uniprot.org/uniprot/Q8IX05"},{"id":"T7","span":{"begin":469,"end":483},"obj":"http://www.uniprot.org/uniprot/Q9UMR7"},{"id":"T8","span":{"begin":469,"end":483},"obj":"http://www.uniprot.org/uniprot/Q8N1N0"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
uniprot-mouse
{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":138,"end":150},"obj":"http://www.uniprot.org/uniprot/Q8BUV3"},{"id":"T2","span":{"begin":149,"end":159},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T3","span":{"begin":307,"end":317},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T4","span":{"begin":674,"end":684},"obj":"http://www.uniprot.org/uniprot/Q00690"},{"id":"T5","span":{"begin":854,"end":864},"obj":"http://www.uniprot.org/uniprot/Q00690"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
GlycoBiology-NCBITAXON
{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":464,"end":468},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9973"},{"id":"T2","span":{"begin":829,"end":839},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/127244"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
sentences
{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":102,"end":222},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":223,"end":557},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":558,"end":896},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":897,"end":1119},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1120,"end":1383},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":222},"obj":"Sentence"},{"id":"T3","span":{"begin":223,"end":557},"obj":"Sentence"},{"id":"T4","span":{"begin":558,"end":896},"obj":"Sentence"},{"id":"T5","span":{"begin":897,"end":1119},"obj":"Sentence"},{"id":"T6","span":{"begin":1120,"end":1383},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":222},"obj":"Sentence"},{"id":"T3","span":{"begin":223,"end":557},"obj":"Sentence"},{"id":"T4","span":{"begin":558,"end":896},"obj":"Sentence"},{"id":"T5","span":{"begin":897,"end":1119},"obj":"Sentence"},{"id":"T6","span":{"begin":1120,"end":1383},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
GO-BP
{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":402,"end":408},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T2","span":{"begin":733,"end":739},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T3","span":{"begin":1095,"end":1101},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T4","span":{"begin":428,"end":430},"obj":"http://purl.obolibrary.org/obo/GO_0033968"},{"id":"T5","span":{"begin":1263,"end":1265},"obj":"http://purl.obolibrary.org/obo/GO_0033968"},{"id":"T6","span":{"begin":1365,"end":1374},"obj":"http://purl.obolibrary.org/obo/GO_0046960"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
GO-MF
{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":29,"end":36},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":182,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":240,"end":247},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":331,"end":338},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":843,"end":850},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T6","span":{"begin":911,"end":918},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T7","span":{"begin":1028,"end":1035},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T8","span":{"begin":1111,"end":1118},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T9","span":{"begin":377,"end":381},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T10","span":{"begin":29,"end":36},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T11","span":{"begin":182,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T12","span":{"begin":240,"end":247},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T13","span":{"begin":331,"end":338},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T14","span":{"begin":843,"end":850},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T15","span":{"begin":911,"end":918},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T16","span":{"begin":1028,"end":1035},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T17","span":{"begin":1111,"end":1118},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T18","span":{"begin":377,"end":381},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T19","span":{"begin":29,"end":36},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T20","span":{"begin":182,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T21","span":{"begin":240,"end":247},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T22","span":{"begin":331,"end":338},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T23","span":{"begin":843,"end":850},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T24","span":{"begin":911,"end":918},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T25","span":{"begin":1028,"end":1035},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T26","span":{"begin":1111,"end":1118},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T27","span":{"begin":377,"end":381},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T28","span":{"begin":29,"end":36},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T29","span":{"begin":182,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T30","span":{"begin":240,"end":247},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T31","span":{"begin":331,"end":338},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T32","span":{"begin":843,"end":850},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T33","span":{"begin":911,"end":918},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T34","span":{"begin":1028,"end":1035},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T35","span":{"begin":1111,"end":1118},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T36","span":{"begin":377,"end":381},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T37","span":{"begin":40,"end":48},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T38","span":{"begin":151,"end":159},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T39","span":{"begin":309,"end":317},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T40","span":{"begin":386,"end":394},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T41","span":{"begin":676,"end":684},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T42","span":{"begin":702,"end":710},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T43","span":{"begin":856,"end":864},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T44","span":{"begin":223,"end":231},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T45","span":{"begin":897,"end":905},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T46","span":{"begin":49,"end":56},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T47","span":{"begin":395,"end":401},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T48","span":{"begin":174,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0005537"},{"id":"T49","span":{"begin":232,"end":247},"obj":"http://purl.obolibrary.org/obo/GO_0005537"},{"id":"T50","span":{"begin":323,"end":338},"obj":"http://purl.obolibrary.org/obo/GO_0005537"},{"id":"T51","span":{"begin":1020,"end":1035},"obj":"http://purl.obolibrary.org/obo/GO_0005537"},{"id":"T52","span":{"begin":182,"end":197},"obj":"http://purl.obolibrary.org/obo/GO_0005515"},{"id":"T53","span":{"begin":240,"end":255},"obj":"http://purl.obolibrary.org/obo/GO_0005515"},{"id":"T54","span":{"begin":331,"end":346},"obj":"http://purl.obolibrary.org/obo/GO_0005515"},{"id":"T55","span":{"begin":1028,"end":1043},"obj":"http://purl.obolibrary.org/obo/GO_0005515"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
UBERON-AE
{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":168,"end":173},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
EDAM-topics
{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":69,"end":81},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":113,"end":125},"obj":"http://edamontology.org/topic_0152"},{"id":"T3","span":{"begin":190,"end":197},"obj":"http://edamontology.org/topic_0078"},{"id":"T4","span":{"begin":248,"end":255},"obj":"http://edamontology.org/topic_0078"},{"id":"T5","span":{"begin":292,"end":301},"obj":"http://edamontology.org/topic_0080"},{"id":"T6","span":{"begin":292,"end":301},"obj":"http://edamontology.org/topic_3168"},{"id":"T7","span":{"begin":339,"end":346},"obj":"http://edamontology.org/topic_0078"},{"id":"T8","span":{"begin":537,"end":547},"obj":"http://edamontology.org/topic_0154"},{"id":"T9","span":{"begin":716,"end":727},"obj":"http://edamontology.org/topic_0602"},{"id":"T10","span":{"begin":1036,"end":1043},"obj":"http://edamontology.org/topic_0078"},{"id":"T11","span":{"begin":1207,"end":1219},"obj":"http://edamontology.org/topic_0152"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
EDAM-DFO
{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":82,"end":93},"obj":"http://edamontology.org/operation_2423"},{"id":"T2","span":{"begin":126,"end":137},"obj":"http://edamontology.org/operation_2423"},{"id":"T3","span":{"begin":190,"end":197},"obj":"http://edamontology.org/data_1467"},{"id":"T4","span":{"begin":190,"end":197},"obj":"http://edamontology.org/format_1208"},{"id":"T5","span":{"begin":211,"end":221},"obj":"http://edamontology.org/data_0883"},{"id":"T6","span":{"begin":248,"end":255},"obj":"http://edamontology.org/data_1467"},{"id":"T7","span":{"begin":248,"end":255},"obj":"http://edamontology.org/format_1208"},{"id":"T8","span":{"begin":292,"end":301},"obj":"http://edamontology.org/operation_3218"},{"id":"T9","span":{"begin":292,"end":301},"obj":"http://edamontology.org/data_2044"},{"id":"T10","span":{"begin":339,"end":346},"obj":"http://edamontology.org/data_1467"},{"id":"T11","span":{"begin":339,"end":346},"obj":"http://edamontology.org/format_1208"},{"id":"T12","span":{"begin":548,"end":556},"obj":"http://edamontology.org/data_1756"},{"id":"T13","span":{"begin":612,"end":620},"obj":"http://edamontology.org/operation_2945"},{"id":"T14","span":{"begin":630,"end":640},"obj":"http://edamontology.org/operation_3429"},{"id":"T15","span":{"begin":685,"end":696},"obj":"http://edamontology.org/operation_2246"},{"id":"T16","span":{"begin":790,"end":800},"obj":"http://edamontology.org/data_0883"},{"id":"T17","span":{"begin":790,"end":809},"obj":"http://edamontology.org/data_1070"},{"id":"T18","span":{"begin":1036,"end":1043},"obj":"http://edamontology.org/format_1208"},{"id":"T19","span":{"begin":1036,"end":1043},"obj":"http://edamontology.org/data_1467"},{"id":"T20","span":{"begin":1159,"end":1171},"obj":"http://edamontology.org/data_0883"},{"id":"T21","span":{"begin":1220,"end":1231},"obj":"http://edamontology.org/operation_2423"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
GlycoBiology-Motifs
{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":402,"end":414},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T2","span":{"begin":733,"end":745},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T3","span":{"begin":1095,"end":1107},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T4","span":{"begin":402,"end":416},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T5","span":{"begin":733,"end":747},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T6","span":{"begin":1095,"end":1109},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T7","span":{"begin":409,"end":414},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T8","span":{"begin":740,"end":745},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T9","span":{"begin":1102,"end":1107},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T10","span":{"begin":409,"end":416},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T11","span":{"begin":740,"end":747},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T12","span":{"begin":1102,"end":1109},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
Lectin
{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":40,"end":48},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T2","span":{"begin":151,"end":159},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T3","span":{"begin":309,"end":317},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T4","span":{"begin":386,"end":394},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T5","span":{"begin":676,"end":684},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T6","span":{"begin":702,"end":710},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T7","span":{"begin":856,"end":864},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T8","span":{"begin":1011,"end":1019},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T9","span":{"begin":40,"end":48},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T10","span":{"begin":149,"end":159},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T11","span":{"begin":307,"end":317},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T12","span":{"begin":386,"end":394},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T13","span":{"begin":674,"end":684},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T14","span":{"begin":702,"end":710},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T15","span":{"begin":854,"end":864},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T16","span":{"begin":1011,"end":1019},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T17","span":{"begin":40,"end":48},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T18","span":{"begin":151,"end":159},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T19","span":{"begin":309,"end":317},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T20","span":{"begin":386,"end":394},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T21","span":{"begin":676,"end":684},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T22","span":{"begin":702,"end":710},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T23","span":{"begin":856,"end":864},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T24","span":{"begin":1011,"end":1019},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T25","span":{"begin":428,"end":430},"obj":"https://acgg.asia/db/lfdb/LfDB0227"},{"id":"Lectin_T26","span":{"begin":1263,"end":1265},"obj":"https://acgg.asia/db/lfdb/LfDB0227"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
GlycoBiology-Epitope
{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":409,"end":416},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":740,"end":747},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":1102,"end":1109},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":402,"end":414},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":733,"end":745},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":1095,"end":1107},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T7","span":{"begin":402,"end":416},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T8","span":{"begin":733,"end":747},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T9","span":{"begin":1095,"end":1109},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
performance-test
{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":168,"end":173},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
Lectin-Jamboree
{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":476,"end":483},"obj":"lectin"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
Lectin-Jamboree-Sentence
{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":222},"obj":"Sentence"},{"id":"T3","span":{"begin":223,"end":557},"obj":"Sentence"},{"id":"T4","span":{"begin":558,"end":896},"obj":"Sentence"},{"id":"T5","span":{"begin":897,"end":1119},"obj":"Sentence"},{"id":"T6","span":{"begin":1120,"end":1383},"obj":"Sentence"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}
NCBITAXON
{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":164,"end":167},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"}],"text":"Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.\nThe C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures. Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues. Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different. Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding. These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite."}