Abstract：
: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.
journal_name
Naturejournal_title
Natureauthors
Weis WI,Drickamer K,Hendrickson WAdoi
10.1038/360127a0keywords:
subject
Has Abstractpub_date
1992-11-12 00:00:00pages
127-34issue
6400eissn
0028-0836issn
1476-4687journal_volume
360pub_type
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