Preparing your results
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
Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.
SciCrunch is a data sharing and display platform. Anyone can create a custom portal where they can select searchable subsets of hundreds of data sources, brand their web pages and create their community. SciCrunch will push data updates automatically to all portals on a weekly basis. User communities can also add their own data to SciCrunch, however this is not currently a free service.
