View source for 3kqr


==The structure of serum amyloid p component bound to phosphoethanolamine==
<StructureSection load='3kqr' size='340' side='right'caption='[[3kqr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3kqr]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KQR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OPE:PHOSPHORIC+ACID+MONO-(2-AMINO-ETHYL)+ESTER'>OPE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kqr OCA], [https://pdbe.org/3kqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kqr RCSB], [https://www.ebi.ac.uk/pdbsum/3kqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kqr ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/SAMP_HUMAN SAMP_HUMAN] Note=SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits.
== Function ==
[https://www.uniprot.org/uniprot/SAMP_HUMAN 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The normal physiological roles of the phylogenetically conserved human plasma proteins C-reactive protein (CRP) and serum amyloid P component (SAP) are not known. Novel drugs targeting their ligand specificities are in clinical development as both proteins have significant pathophysiological effects, SAP in promoting amyloidosis and CRP in exacerbating ischemic injury. Both proteins bind to phosphoethanolamine and we show here that, under physiological conditions, phosphoethanolamine is bound with higher affinity by human SAP than by human CRP. An explanation is provided by X-ray crystal structures that show SAP residue Tyr74 allowing additional hydrophobic protein-ligand interactions compared with the equivalent Thr76 of CRP. Docking simulations show many more low energy positions for phosphoethanolamine bound by CRP than by SAP and are consistent with the crystallographic and functional binding results. These fundamental observations on structure-activity relationships will aid the design of improved pentraxin targeting drugs. Copyright (c) 2011 John Wiley &amp; Sons, Ltd.

Structural basis of ligand specificity in the human pentraxins, C-reactive protein and serum amyloid P component.,Mikolajek H, Kolstoe SE, Pye VE, Mangione P, Pepys MB, Wood SP J Mol Recognit. 2011 Mar;24(2):371-7. doi: 10.1002/jmr.1090. PMID:21360619<ref>PMID:21360619</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3kqr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Serum amyloid P-component|Serum amyloid P-component]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kolstoe SE]]
[[Category: Mikolajek H]]
[[Category: Pepys MB]]
[[Category: Wood SP]]