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Structural basis of carbohydrate recognition by a Man(alpha1-2)Man-specific lectin from Bowringia milbraedii
Publication Type:
Journal ArticleSource:
Volume 16, Issue 7, p.635 - 640 (2006)URL:
PM:16567368Keywords:
Binding Sites; Carbohydrates; chemistry; Crystallography; X-Ray; Dimerization; Disaccharides; Fabaceae; metabolism; Mannose-Binding Lectins; Mannosides; Plant Lectins; Protein Structure; Quaternary; Seeds; SolutionsAbstract:
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
Notes:
DA - 20060616
IS - 0959-6658 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Carbohydrates)
RN - 0 (Disaccharides)
RN - 0 (Mannose-Binding Lectins)
RN - 0 (Mannosides)
RN - 0 (Plant Lectins)
RN - 0 (Solutions)
RN - 0 (mannosyl alpha(1-6)-mannoside)
SB - IM