Abstract
C-type (Ca2+-dependent) animal lectins such as mannose-binding proteins mediate many cell-surface carbohydrate-recognition events. The crystal structure at 1.7 Å 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.
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Weis, W., Drickamer, K. & Hendrickson, W. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360, 127–134 (1992). https://doi.org/10.1038/360127a0
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DOI: https://doi.org/10.1038/360127a0
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