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Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil

Nature Structural Biology volume 1, pages 789–794 (1994)Cite this article

A Corrigendum to this article was published on 01 January 1996

Abstract

Human mannose-binding protein is a hexamer of trimers with each subunit consisting of an amino-terminal region rich in cysteine, 19 collagen repeats, a ‘neck’, and a carbohydrate recognition domain that requires calcium to bind ligand. A 148-residue peptide, consisting of the ‘neck’ and carbohydrate recognition domains forms trimers in solution and in crystals. The structure of this trimeric peptide has been determined in two different crystal forms. The ‘neck’ forms a triple α-helical coiled-coil. Each α-helix interacts with a neighbouring carbohydrate recognition domain. The spatial arrangement of the carbohydrate recognition domains suggest how MBP trimers form the basic recognition unit for branched oligosaccharides on microorganisms.

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Authors and Affiliations

  1. Bristol-Myers Squibb Pharmaceutical Research Institute, P.O. Box 4000, Princeton, NJ, 08543-4000, USA

    Steven Sheriff & ChiehYing Y. Chang

  2. Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute, Boston, MA, 02115, USA

    R. Alan B. Ezekowitz

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  1. Steven Sheriff
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  2. ChiehYing Y. Chang
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  3. R. Alan B. Ezekowitz
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Sheriff, S., Chang, C. & Ezekowitz, R. Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil. Nat Struct Mol Biol 1, 789–794 (1994). https://doi.org/10.1038/nsb1194-789

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