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Three dimensional structure of human C-reactive protein

Nature Structural Biology volume 3, pages 346–354 (1996)Cite this article

Abstract

The structure of the classical acute phase reactant human C-reactive protein provides evidence that phosphocholine binding is mediated through calcium and a hydrophobic pocket centred on Phe 66. The residue Glu 81 is suitably positioned to interact with the choline group. A cleft on the pentameric face opposite to that containing the calcium site may have an important functional role. The structure provides insights into the molecular mechanisms by which this highly conserved plasma protein, for which no polymorphism or deficiency state is known, may exert its biological role.

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Author notes

  1. Graham M.T. Gheetham

    Present address: Department of Molecular Biophysics and Biochemistry, Yale University, Bass Center, 266 Whitney Avenue, P.O. Box 208114, Newhaven, Connecitcut, 06250, USA

  2. William G. Turnell

    Present address: Biologie, L'ecole Superieure de Physique et Chimie Industrielles (ESPCI) de la Ville de Paris, 10 rue Vauquelin, 75231, Paris, Cedex 5, France

Authors and Affiliations

  1. Department of Physics, Keele University, Keele, Staffs, ST55BG, UK

    Annette K. Shrive, David Holden, Dean A.A. Myles & Trevor J. Greenhough

  2. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Graham M.T. Gheetham, William G. Turnell & Anne C. Bloomer

  3. Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, W12 QNN, UK

    William G. Turnell & Mark B. Pepys

  4. Division of Clinical Immunology and Rheumatology, Department of Medicine, University of Alabama in Birmingham, Birmingham, Alabama, 35294, USA

    John E. Volanakis

  5. CCLRC Daresbury Laboratory, Daresbury, Warrington, WA44AD, UK

    Trevor J. Greenhough

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Shrive, A., Gheetham, G., Holden, D. et al. Three dimensional structure of human C-reactive protein. Nat Struct Mol Biol 3, 346–354 (1996). https://doi.org/10.1038/nsb0496-346

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