Title | Structural basis of carbohydrate recognition by a Man(alpha1-2)Man-specific lectin from Bowringia milbraedii. |
Publication Type | Journal Article |
Year of Publication | 2006 |
Authors | Buts, L., A. Garcia-Pino, L. Wyns, and R. Loris |
Journal | Glycobiology |
Volume | 16 |
Issue | 7 |
Pagination | 635-40 |
Date Published | 2006 Jul |
Type of Article | lectins |
ISSN | 0959-6658 |
Keywords | Binding Sites, Carbohydrates, Crystallography, X-Ray, Dimerization, Disaccharides, Fabaceae, Mannose-Binding Lectins, Mannosides, Plant Lectins, Protein Structure, Quaternary, Seeds, Solutions |
Abstract | The crystal structure of the seed lectin from the tropical legume Bowringia milbraedii was determined in complex with the disaccharide ligand Man(alpha1-2)Man. In solution, the protein exhibits a dynamic dimer-tetramer equilibrium, consistent with the concanavalin A-type tetramer observed in the crystal. Contacts between the tetramers are mediated almost exclusively through the carbohydrate ligand, resulting in a crystal lattice virtually identical to that of the concanavalin-A:Man(alpha1-2)Man complex, even though both proteins have less than 50% sequence identity. The disaccharide binds exclusively in a "downstream" binding mode, with the non-reducing mannose occupying the monosaccharide-binding site. The reducing mannose is bound in a predominantly polar subsite involving Tyr131, Gln218, and Tyr219. |
DOI | 10.1093/glycob/cwj109 |
Alternate Journal | Glycobiology |
PubMed ID | 16567368 |
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