Nature Structural Biology
3, 346 - 354 (1996)
doi:10.1038/nsb0496-346
Three dimensional structure of human C-reactive proteinAnnette K. Shrive1, Graham M.T. Gheetham2, 6, David Holden1, Dean A.A. Myles1, William G. Turnell2, 3, 7, John E. Volanakis4, Mark B. Pepys3, Anne C. Bloomer2
& Trevor J. Greenhough1, 5
1Department of Physics, Keele University, Keele, Staffs ST55BG, UK
2 MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
3Immunological Medicine Unit, Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London W12 QNN, UK
4Division of Clinical Immunology and Rheumatology, Department of Medicine, University of Alabama in Birmingham, Birmingham, Alabama 35294, USA
5CCLRC Daresbury Laboratory, Daresbury, WarringtonWA44AD, UK
6Present address: Department of Molecular Biophysics and Biochemistry, Yale University, Bass Center, 266 Whitney Avenue, P.O. Box 208114, Newhaven, Connecitcut 06250, USA
7Present address: Biologie, L'ecole Superieure de Physique etChimielndustrielles (ESPCI)delaVillede Paris, 10rueVauquelin, 75231 Paris Cedex5, France 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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