3l2y: Difference between revisions
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<StructureSection load='3l2y' size='340' side='right'caption='[[3l2y]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3l2y' size='340' side='right'caption='[[3l2y]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3l2y]] is a 20 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3l2y]] is a 20 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=3L2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L2Y FirstGlance]. <br> | ||
</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=OPE:PHOSPHORIC+ACID+MONO-(2-AMINO-ETHYL)+ESTER'>OPE</scene></td></tr> | </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=OPE:PHOSPHORIC+ACID+MONO-(2-AMINO-ETHYL)+ESTER'>OPE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b09|1b09]], [[1gnh|1gnh]], [[1lj7|1lj7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b09|1b09]], [[1gnh|1gnh]], [[1lj7|1lj7]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l2y OCA], [https://pdbe.org/3l2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l2y RCSB], [https://www.ebi.ac.uk/pdbsum/3l2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l2y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CRP_HUMAN CRP_HUMAN]] Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3l2y" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3l2y" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[C-reactive protein|C-reactive protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 08:40, 13 July 2022
The structure of C-reactive protein bound to phosphoethanolamineThe structure of C-reactive protein bound to phosphoethanolamine
Structural highlights
Function[CRP_HUMAN] Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. Publication Abstract from PubMedThe 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 & 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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