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19 April 2024

» pubmed » pmid8114934

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Structure of pentameric human serum amyloid P component
J Emsley ; H E White ; B P O’Hara ; G Oliva ; N Srinivasan ; I J Tickle ; T L Blundell ; M B Pepys ; S P Wood ;
Date:	27 Jan 1994
Journal:	Nature, 367 (6461), 338-45
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 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.
Source:	PubMed, pmid8114934 doi: 10.1038/367338a0
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