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Structure of pentameric human serum amyloid P component.

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


  • Emsley J
  • White HE
  • O'Hara BP
  • Oliva G
  • Srinivasan N
  • Tickle IJ
  • Blundell TL
  • Pepys MB
  • Wood SP



Publication Data

January 27, 1994

Associated Grants


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