Structure of pentameric human serum amyloid P component

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

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)338-345
Issue number6461
Publication statusPublished - 27 Jan 1994


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