Structural highlights
Disease
SAMP_HUMAN Note=SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits.
Function
SAMP_HUMAN Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of pentameric human serum amyloid P component.,Emsley J, White HE, O'Hara BP, Oliva G, Srinivasan N, Tickle IJ, Blundell TL, Pepys MB, Wood SP Nature. 1994 Jan 27;367(6461):338-45. PMID:8114934[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Emsley J, White HE, O'Hara BP, Oliva G, Srinivasan N, Tickle IJ, Blundell TL, Pepys MB, Wood SP. Structure of pentameric human serum amyloid P component. Nature. 1994 Jan 27;367(6461):338-45. PMID:8114934 doi:http://dx.doi.org/10.1038/367338a0
