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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 ID: 8114934 RIS Download
Mesh terms: Amino Acid Sequence | Amyloidosis | Binding Sites | C-Reactive Protein | Calcium | Computer Graphics | Crystallography, X-Ray | DNA | Endopeptidases | Humans | Ligands | Methylgalactosides | Models, Molecular | Molecular Sequence Data | Phosphatidylethanolamines | Phosphorylcholine | Protein Conformation | Protein Folding | Protein Structure, Secondary | Sequence Alignment | Serum Amyloid P-Component
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