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'''THE STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID P COMPONENT''' | '''THE STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID P COMPONENT''' | ||
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[[Category: White, H E.]] | [[Category: White, H E.]] | ||
[[Category: Wood, S P.]] | [[Category: Wood, S P.]] | ||
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Revision as of 05:28, 3 May 2008
THE STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID P COMPONENT
Overview
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.
About this Structure
1SAC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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, Nature. 1994 Jan 27;367(6461):338-45. PMID:8114934 Page seeded by OCA on Sat May 3 08:28:57 2008
