|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|
|Date Published||2006 Jul|
|Type of Article||lectins|
|Keywords||Binding Sites, Carbohydrates, Crystallography, X-Ray, Dimerization, Disaccharides, Fabaceae, Mannose-Binding Lectins, Mannosides, Plant Lectins, Protein Structure, Quaternary, Seeds, Solutions|
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.