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1SAC

THE STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID P COMPONENT

Summary for 1SAC
Entry DOI10.2210/pdb1sac/pdb
DescriptorSERUM AMYLOID P COMPONENT, CALCIUM ION, ACETIC ACID (3 entities in total)
Functional Keywordsamyloid protein
Biological sourceHomo sapiens (human)
Total number of polymer chains5
Total formula weight117053.26
Authors
White, H.E.,Emsley, J.,O'Hara, B.P.,Oliva, G.,Srinivasan, N.,Tickle, I.J.,Blundell, T.L.,Pepys, M.B.,Wood, S.P. (deposition date: 1994-01-27, release date: 1994-05-31, Last modification date: 2024-11-20)
Primary citationEmsley, J.,White, H.E.,O'Hara, B.P.,Oliva, G.,Srinivasan, N.,Tickle, I.J.,Blundell, T.L.,Pepys, M.B.,Wood, S.P.
Structure of pentameric human serum amyloid P component.
Nature, 367:338-345, 1994
Cited by
PubMed 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.
PubMed: 8114934
DOI: 10.1038/367338a0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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