PubMed:26715202 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":49,"end":52},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T2","span":{"begin":49,"end":52},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T3","span":{"begin":519,"end":522},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T4","span":{"begin":519,"end":522},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T5","span":{"begin":857,"end":860},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T6","span":{"begin":857,"end":860},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T7","span":{"begin":906,"end":909},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T8","span":{"begin":906,"end":909},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T9","span":{"begin":960,"end":963},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T10","span":{"begin":960,"end":963},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T11","span":{"begin":1252,"end":1255},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T12","span":{"begin":1252,"end":1255},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T13","span":{"begin":1301,"end":1304},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T14","span":{"begin":1301,"end":1304},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":49,"end":52},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":519,"end":522},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":857,"end":860},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":906,"end":909},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":960,"end":963},"obj":"Glycan_Motif"},{"id":"T11","span":{"begin":1252,"end":1255},"obj":"Glycan_Motif"},{"id":"T13","span":{"begin":1301,"end":1304},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A8","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A10","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A11","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A12","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A13","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A14","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":49,"end":52},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T2","span":{"begin":519,"end":522},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T3","span":{"begin":857,"end":860},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T4","span":{"begin":906,"end":909},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T5","span":{"begin":960,"end":963},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T6","span":{"begin":1252,"end":1255},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"T7","span":{"begin":1301,"end":1304},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":91},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":92,"end":268},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":269,"end":475},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":476,"end":716},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":717,"end":1022},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1023,"end":1232},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1233,"end":1511},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":91},"obj":"Sentence"},{"id":"T2","span":{"begin":92,"end":268},"obj":"Sentence"},{"id":"T3","span":{"begin":269,"end":475},"obj":"Sentence"},{"id":"T4","span":{"begin":476,"end":716},"obj":"Sentence"},{"id":"T5","span":{"begin":717,"end":1022},"obj":"Sentence"},{"id":"T6","span":{"begin":1023,"end":1232},"obj":"Sentence"},{"id":"T7","span":{"begin":1233,"end":1511},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":91},"obj":"Sentence"},{"id":"T2","span":{"begin":92,"end":268},"obj":"Sentence"},{"id":"T3","span":{"begin":269,"end":475},"obj":"Sentence"},{"id":"T4","span":{"begin":476,"end":716},"obj":"Sentence"},{"id":"T5","span":{"begin":717,"end":1022},"obj":"Sentence"},{"id":"T6","span":{"begin":1023,"end":1232},"obj":"Sentence"},{"id":"T7","span":{"begin":1233,"end":1511},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":49,"end":52},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T2","span":{"begin":49,"end":52},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T3","span":{"begin":519,"end":522},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T4","span":{"begin":519,"end":522},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T5","span":{"begin":857,"end":860},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T6","span":{"begin":857,"end":860},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T7","span":{"begin":906,"end":909},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T8","span":{"begin":906,"end":909},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T9","span":{"begin":960,"end":963},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T10","span":{"begin":960,"end":963},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T11","span":{"begin":1252,"end":1255},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T12","span":{"begin":1252,"end":1255},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T13","span":{"begin":1301,"end":1304},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T14","span":{"begin":1301,"end":1304},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":49,"end":52},"obj":"Glycan"},{"id":"T2","span":{"begin":519,"end":522},"obj":"Glycan"},{"id":"T3","span":{"begin":857,"end":860},"obj":"Glycan"},{"id":"T4","span":{"begin":906,"end":909},"obj":"Glycan"},{"id":"T5","span":{"begin":960,"end":963},"obj":"Glycan"},{"id":"T6","span":{"begin":1252,"end":1255},"obj":"Glycan"},{"id":"T7","span":{"begin":1301,"end":1304},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G48558GR"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":53,"end":64},"obj":"FMAID:82816"},{"id":"_T2","span":{"begin":53,"end":64},"obj":"FMAID:196811"},{"id":"_T3","span":{"begin":102,"end":115},"obj":"FMAID:212684"},{"id":"_T4","span":{"begin":102,"end":115},"obj":"FMAID:200942"},{"id":"_T5","span":{"begin":107,"end":115},"obj":"FMAID:50594"},{"id":"_T6","span":{"begin":107,"end":115},"obj":"FMAID:146300"},{"id":"_T7","span":{"begin":523,"end":534},"obj":"FMAID:82816"},{"id":"_T8","span":{"begin":523,"end":534},"obj":"FMAID:196811"},{"id":"_T9","span":{"begin":538,"end":546},"obj":"FMAID:226028"},{"id":"_T10","span":{"begin":538,"end":546},"obj":"FMAID:226027"},{"id":"_T11","span":{"begin":615,"end":623},"obj":"FMAID:67257"},{"id":"_T12","span":{"begin":615,"end":623},"obj":"FMAID:165447"},{"id":"_T13","span":{"begin":663,"end":675},"obj":"FMAID:61795"},{"id":"_T14","span":{"begin":663,"end":675},"obj":"FMAID:165243"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":723,"end":726},"obj":"http://www.uniprot.org/uniprot/Q06520"},{"id":"T2","span":{"begin":821,"end":823},"obj":"http://www.uniprot.org/uniprot/P07954"},{"id":"T3","span":{"begin":1142,"end":1144},"obj":"http://www.uniprot.org/uniprot/P07954"},{"id":"T4","span":{"begin":1292,"end":1294},"obj":"http://www.uniprot.org/uniprot/P07954"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":394,"end":401},"obj":"http://www.uniprot.org/uniprot/Q9EQE5"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":24,"end":36},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11642"},{"id":"T2","span":{"begin":24,"end":36},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/46771"},{"id":"T3","span":{"begin":24,"end":39},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/585074"},{"id":"T4","span":{"begin":24,"end":39},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/10633"},{"id":"T5","span":{"begin":31,"end":36},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/184751"},{"id":"T6","span":{"begin":992,"end":1004},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11642"},{"id":"T7","span":{"begin":992,"end":1004},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/46771"},{"id":"T8","span":{"begin":992,"end":1007},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/10633"},{"id":"T9","span":{"begin":992,"end":1007},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/585074"},{"id":"T10","span":{"begin":999,"end":1004},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/184751"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":179,"end":190},"obj":"http://purl.obolibrary.org/obo/GO_0032502"},{"id":"T2","span":{"begin":238,"end":246},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T3","span":{"begin":776,"end":789},"obj":"http://purl.obolibrary.org/obo/GO_0045087"},{"id":"T4","span":{"begin":776,"end":799},"obj":"http://purl.obolibrary.org/obo/GO_0045088"},{"id":"T5","span":{"begin":790,"end":799},"obj":"http://purl.obolibrary.org/obo/GO_0065007"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":40,"end":44},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":825,"end":830},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":910,"end":917},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":964,"end":971},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":40,"end":44},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T6","span":{"begin":825,"end":830},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T7","span":{"begin":910,"end":917},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T8","span":{"begin":964,"end":971},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T9","span":{"begin":40,"end":44},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T10","span":{"begin":825,"end":830},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T11","span":{"begin":910,"end":917},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T12","span":{"begin":964,"end":971},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T13","span":{"begin":40,"end":44},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T14","span":{"begin":825,"end":830},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T15","span":{"begin":910,"end":917},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T16","span":{"begin":964,"end":971},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T17","span":{"begin":596,"end":602},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":102,"end":106},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":102,"end":115},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":49,"end":52},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":519,"end":522},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":857,"end":860},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":906,"end":909},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":960,"end":963},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":1252,"end":1255},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"PD-GlycoEpitope-B_T7","span":{"begin":1301,"end":1304},"obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":723,"end":726},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0021681"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":24,"end":39},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":992,"end":1007},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1009,"end":1013},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1283,"end":1287},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1891767"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1891767"},{"id":"A3","pred":"db_id","subj":"T3","obj":"1891767"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1891767"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"Glycosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":49,"end":52},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":519,"end":522},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":857,"end":860},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":906,"end":909},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":960,"end":963},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1252,"end":1255},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1301,"end":1304},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":343,"end":348},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000464"}],"text":"Complement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformations.\nMammalian cell surfaces are decorated with a variety of glycan chains that orchestrate development and defense and are exploited by pathogens for cellular attachment and entry. While glycosidic linkages are, in principle, flexible, the conformational space that a given glycan can sample is subject to spatial and electrostatic restrictions imposed by its overall chemical structure. Here, we show how the glycan moiety of the GM1 ganglioside, a branched, monosialylated pentasaccharide that serves as a ligand for various proteins, undergoes differential conformational selection in its interactions with different lectins. Using STD NMR and X-ray crystallography, we found that the innate immune regulator Complement Factor H (FH) binds a previously not reported GM1 conformation that is not compatible with the GM1 binding sites of other structurally characterized GM1-binding lectins such as the Simian Virus 40 (SV40) capsid. Molecular dynamics simulations of the free glycan in explicit solvent on the ten microsecond timescale reveal that the FH-bound conformation nevertheless corresponds to a minimum in the Gibbs free energy plot. In contrast to the GM1 conformation recognized by SV40 the FH-bound GM1 conformation is associated with poor NOE restraints, explaining how it escaped (1)H-(1)H NOE restrained modeling in the past and highlighting the necessity for ensemble representations of glycan structures."}