1SAC
THE STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID P COMPONENT
Summary for 1SAC
Entry DOI | 10.2210/pdb1sac/pdb |
Descriptor | SERUM AMYLOID P COMPONENT, CALCIUM ION, ACETIC ACID (3 entities in total) |
Functional Keywords | amyloid protein |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 5 |
Total formula weight | 117053.26 |
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 citation | Emsley, 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: 8114934DOI: 10.1038/367338a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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