2msb

Publication Abstract from PubMed

C-type (Ca(2+)-dependent) animal lectins such as mannose-binding proteins mediate many cell-surface carbohydrate-recognition events. The crystal structure at 1.7 A resolution of the carbohydrate-recognition domain of rat mannose-binding protein complexed with an oligomannose asparaginyl-oligosaccharide reveals that Ca2+ forms coordination bonds with the carbohydrate ligand. Carbohydrate specificity is determined by a network of coordination and hydrogen bonds that stabilizes the ternary complex of protein, Ca2+ and sugar. Two branches of the oligosaccharide crosslink neighbouring carbohydrate-recognition domains in the crystal, enabling multivalent binding to a single oligosaccharide chain to be visualized directly.

Structure of a C-type mannose-binding protein complexed with an oligosaccharide.,Weis WI, Drickamer K, Hendrickson WA Nature. 1992 Nov 12;360(6400):127-34. PMID:1436090^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.