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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acetylglucosamine / metabolism
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Animals
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Asparagine / analogs & derivatives*
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Asparagine / chemistry
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Asparagine / metabolism
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Calcium / metabolism*
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism*
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Crystallography
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Fucose / metabolism
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Glucose / metabolism
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Mannose / metabolism
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Mannose-Binding Lectin*
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Models, Molecular
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Molecular Conformation
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Molecular Structure
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Oligosaccharides / chemistry*
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Oligosaccharides / metabolism*
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Rats
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Substrate Specificity
Substances
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Carrier Proteins
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Mannose-Binding Lectin
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Oligosaccharides
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mannose binding protein A
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Fucose
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(mannose)6-(N-acetylglucosamine)2-asparagine
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Asparagine
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Glucose
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Mannose
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Calcium
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Acetylglucosamine