STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE

被引:861
作者
WEIS, WI
DRICKAMER, K
HENDRICKSON, WA
机构
[1] COLUMBIA UNIV, DEPT BIOCHEM & MOLEC BIOPHYS, NEW YORK, NY 10032 USA
[2] COLUMBIA UNIV, HOWARD HUGHES MED INST, NEW YORK, NY 10032 USA
关键词
D O I
10.1038/360127a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
C-type (Ca2+-dependent) animal lectins such as mannose-binding proteins mediate many cell-surface carbohydrate-recognition events. The crystal structure at 1.7 angstrom 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.
引用
收藏
页码:127 / 134
页数:8
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