| http://purl.uniprot.org/citations/1321144 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1321144 | http://www.w3.org/2000/01/rdf-schema#comment | "The crystal structure of wheat germ agglutinin isolectin 1 (WGA1) complexed with a tryptic sialoglycopeptide fragment (T-5) from its erythrocyte receptor glycophorin A, which contains the O-linked tetrasaccharide NeuNAc-alpha 2,3-Gal-beta 1,3-(alpha 2,6-NeuNAc) Gal-NAc-alpha 1-O-Thr, has been determined by molecular replacement techniques and refined at 2.0-A resolution (R = 18.1%). The structure reveals that association between WGA1 dimers, composed of two identical four-domain (A-D) monomers, and T-5 is asymmetric and involves sialic acid binding at three nonequivalent aromatic residue-rich sites. Two independent binding modes are observed. In the dominant ("major") binding mode, the two highest affinity sites are utilized to cross-link neighboring crystallographically related WGA1 dimers. The branched tetrasaccharide has an extended rigid conformation, and its terminal alpha 2,6-NeuNAc and alpha 2,3-NeuNAc residues occupy specificity sites in domains B1 (monomer 1) and C2 (monomer 2) on opposing dimers, respectively. This asymmetric selection of binding sites leads to infinite open-ended arrays of interlinked lectin molecules. In the subsidiary "minor" binding mode, only the terminal alpha 2,6-NeuNAc, anchored to the aromatic residue-rich binding site in domain A2, is clearly visible. The remaining portion of T-5 is disordered. This structure presents the first evidence for NeuNAc binding in the aromatic residue-rich sites of domains A and C and suggests a preference of WGA for alpha 2,6-linked NeuNAc. Moreover, the unusual asymmetric WGA1-tetrasaccharide association, involving domain binding sites that differ in their binding affinities for NeuNAc, offers explanations for the widely observed cooperative cell binding behavior of WGA."xsd:string |
| http://purl.uniprot.org/citations/1321144 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)49718-4"xsd:string |
| http://purl.uniprot.org/citations/1321144 | http://purl.uniprot.org/core/author | "Wright C.S."xsd:string |
| http://purl.uniprot.org/citations/1321144 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1321144 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/1321144 | http://purl.uniprot.org/core/pages | "14345-14352"xsd:string |
| http://purl.uniprot.org/citations/1321144 | http://purl.uniprot.org/core/title | "Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex. Structural basis for cooperative lectin-cell binding."xsd:string |
| http://purl.uniprot.org/citations/1321144 | http://purl.uniprot.org/core/volume | "267"xsd:string |
| http://purl.uniprot.org/citations/1321144 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1321144 |
| http://purl.uniprot.org/citations/1321144 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1321144 |
| http://purl.uniprot.org/uniprot/#_P10968-mappedCitation-1321144 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/1321144 |
| http://purl.uniprot.org/uniprot/P10968 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/1321144 |