PubMed:8262940 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"T2","span":{"begin":113,"end":322},"obj":"Sentence"},{"id":"T3","span":{"begin":323,"end":495},"obj":"Sentence"},{"id":"T4","span":{"begin":496,"end":620},"obj":"Sentence"},{"id":"T5","span":{"begin":621,"end":826},"obj":"Sentence"},{"id":"T6","span":{"begin":827,"end":952},"obj":"Sentence"},{"id":"T7","span":{"begin":953,"end":1065},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"T2","span":{"begin":113,"end":322},"obj":"Sentence"},{"id":"T3","span":{"begin":323,"end":495},"obj":"Sentence"},{"id":"T4","span":{"begin":496,"end":620},"obj":"Sentence"},{"id":"T5","span":{"begin":621,"end":826},"obj":"Sentence"},{"id":"T6","span":{"begin":827,"end":952},"obj":"Sentence"},{"id":"T7","span":{"begin":953,"end":1065},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.\nS-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":47,"end":50},"obj":"Glycan"},{"id":"T2","span":{"begin":84,"end":91},"obj":"Glycan"},{"id":"T3","span":{"begin":115,"end":118},"obj":"Glycan"},{"id":"T4","span":{"begin":151,"end":158},"obj":"Glycan"},{"id":"T5","span":{"begin":429,"end":432},"obj":"Glycan"},{"id":"T6","span":{"begin":466,"end":473},"obj":"Glycan"},{"id":"T7","span":{"begin":940,"end":943},"obj":"Glycan"},{"id":"T8","span":{"begin":1053,"end":1056},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A9","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A10","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A11","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A12","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A13","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A14","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A15","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A16","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"}],"text":"X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.\nS-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":47,"end":50},"obj":"Glycan"},{"id":"T2","span":{"begin":84,"end":91},"obj":"Glycan"},{"id":"T3","span":{"begin":115,"end":118},"obj":"Glycan"},{"id":"T4","span":{"begin":151,"end":158},"obj":"Glycan"},{"id":"T5","span":{"begin":429,"end":432},"obj":"Glycan"},{"id":"T6","span":{"begin":466,"end":473},"obj":"Glycan"},{"id":"T7","span":{"begin":940,"end":943},"obj":"Glycan"},{"id":"T8","span":{"begin":1053,"end":1056},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A9","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A10","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A11","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A12","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A13","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A14","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A15","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A16","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"}],"text":"X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.\nS-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":31,"end":36},"obj":"Organism"},{"id":"T2","span":{"begin":413,"end":418},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.\nS-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"T2","span":{"begin":113,"end":322},"obj":"Sentence"},{"id":"T3","span":{"begin":323,"end":495},"obj":"Sentence"},{"id":"T4","span":{"begin":496,"end":620},"obj":"Sentence"},{"id":"T5","span":{"begin":621,"end":826},"obj":"Sentence"},{"id":"T6","span":{"begin":827,"end":952},"obj":"Sentence"},{"id":"T7","span":{"begin":953,"end":1065},"obj":"Sentence"}],"text":"X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.\nS-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"T2","span":{"begin":113,"end":322},"obj":"Sentence"},{"id":"T3","span":{"begin":323,"end":495},"obj":"Sentence"},{"id":"T4","span":{"begin":496,"end":620},"obj":"Sentence"},{"id":"T5","span":{"begin":621,"end":826},"obj":"Sentence"},{"id":"T6","span":{"begin":827,"end":952},"obj":"Sentence"},{"id":"T7","span":{"begin":953,"end":1065},"obj":"Sentence"}],"text":"X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.\nS-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":31,"end":36},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":413,"end":418},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.\nS-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins."}