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Structure of pentameric human serum amyloid P component

Nature volume 367, pages 338–345 (1994)Cite this article

Abstract

The three-dimensional structure of pentameric human serum amyloid P component at high resolution, the first reported for a pentraxin, reveals that the tertiary fold is remarkably similar to that of the legume lectins. Carboxylate and phosphate compounds bind directly to two calcium ions; interactions with a carboxyethylidene ring are mediated by Asn 59 and Gin 148 ligands of the calcium ions. These X-ray results indicate the probable modes of binding of the biologically important ligands, DNA and amyloid fibrils.

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Author notes

  1. Bernard P. O'Hara

    Present address: Department of Biochemistry and Molecular Biology, University College, London, WC1E 6BT, UK

  2. Glaucius Oliva

    Present address: Institute de Fisica e Quimica de Sao Carlos, Departamento de Fisica e Ciencia dos Materials, Universitade de Sao Paulo, Sao Carlos SP, 3560-250, Brazil

  3. Mark B. Pepys: Immunological Medicine Unit, Royal Postgraduate Medical School, Hammersmith Hospital, London W12 ONN, UK

Authors and Affiliations

  1. Laboratory of Molecular Biology and ICRF Unit of Structural Molecular Biology, Department of Crystallography, Birkbeck College, London, WC1E 7HX, UK

    Jonas Emsley, Helen E. White, Bernard P. O'Hara, Glaucius Oliva, Narayanaswamy Srinivasan, Ian J. Tickle, Tom L. Blundell, Mark B. Pepys & Steve P. Wood

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Emsley, J., White, H., O'Hara, B. et al. Structure of pentameric human serum amyloid P component. Nature 367, 338–345 (1994). https://doi.org/10.1038/367338a0

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