Structure of pentameric human serum amyloid P component

• DOI: 10.1038/367338a0
• Publication Date: 2003-08-12T00:54:08Z
• Authors: Jonas Emsley; Helen E. White; Bernard P. O'Hara; Glaucius Oliva; Narayanaswamy Sri...; Ian J. Tickle; Tom L. Blundell; Mark B. Pepys; Steve P. Wood
• Keywords: Amyloid (mycology); Carboxylate

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.