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    Nature. 1994 Jan 27;367(6461):338-45.

    Structure of pentameric human serum amyloid P component.

    Emsley J, White HE, O'Hara BP, Oliva G, Srinivasan N, Tickle IJ, Blundell TL, Pepys MB, Wood SP.

    Laboratory of Molecular Biology, Birkbeck College, London, UK.

    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 Gln 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.

    PMID: 8114934 [PubMed - indexed for MEDLINE]

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