The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL.

Hamelryck, T W; Moore, J G; Chrispeels, M J; Loris, R; Wyns, L

Hamelryck, T W; Moore, J G; Chrispeels, M J; Loris, R; Wyns, L.

Affiliation

Hamelryck TW; Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, Sint-Genesius-Rode, B-1640, Belgium. thamelry@vub.ac.be

J Mol Biol ; 299(4): 875-83, 2000 Jun 16.

Article in En | MEDLINE | ID: mdl-10843844

Subject(s)

Cross-Linking Reagents/metabolism; Fabaceae/chemistry; Lectins/chemistry; Lectins/metabolism; Mannose-Binding Lectins; Plants, Medicinal; Trisaccharides/metabolism; Binding Sites; Carbohydrate Conformation; Carbohydrate Sequence; Concanavalin A/chemistry; Concanavalin A/metabolism; Cross-Linking Reagents/chemistry; Crystallography, X-Ray; Dimerization; Hydrogen Bonding; Mannose/chemistry; Mannose/metabolism; Models, Molecular; Molecular Sequence Data; Plant Lectins; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Substrate Specificity; Trisaccharides/chemistry

Search on Google

XML

PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Plants, Medicinal / Trisaccharides / Cross-Linking Reagents / Mannose-Binding Lectins / Lectins / Fabaceae Language: En Journal: J Mol Biol Year: 2000 Type: Article Affiliation country: Belgium

Search on Google

XML

PubMed Links