Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

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

Structure of pentameric human serum amyloid P component.

Nature | Jan 27, 1994

http://www.ncbi.nlm.nih.gov/pubmed/8114934

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