Abstract
Recognition mechanisms of carbohydrate by animal lectins are reviewed. A lectin focused in this article is a mannan-binding protein or mannose binding protein, MBP, which is present in serum of various mammals and binds specifically to mannose or N-acetylglucosamine residue. MBP is an oligomeric protein consisting of 18 identical subunits of 32 kDa. Each subunit has a carbohydrate recognition domain (CRD) at its COOH-terminal and a collagen like domain at its NH2-terminal. The lectin is shown to be able to activate the complement system and is involved in an immunoglobulin-independent host defense. The low serum levels of MBP are associated with a common opsonic defect. Studies by Dr. Drickamer's group on the crystal structure of CRD of MBP complexed with an oligomannose-type glycopeptides revealed that that carbohydrate specificity is determined by a network of coordination and hydrogen bonds that stabilized the ternary complex of protein, Ca2+ and sugar.
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