• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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