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Structure of a C-type mannose-binding protein complexed with an oligosaccharide

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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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Author notes

  1. William I. Weis

    Present address: Department of Cell Biology, Fairchild Building, Stanford University School of Medicine, Stanford, California, 94305, USA

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168 Street, New York, New York, 10032, USA

    William I. Weis, Kurt Drickamer & Wayne A. Hendrickson

  2. Howard Hughes Medical Institute, Columbia University, 630 West 168 Street, New York, New York, 10032, USA

    William I. Weis & Wayne A. Hendrickson

Authors
  1. William I. Weis
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  2. Kurt Drickamer
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  3. Wayne A. Hendrickson
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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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