3pvn: Difference between revisions
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==Triclinic form of Human C-Reactive Protein in complex with Zinc== | ==Triclinic form of Human C-Reactive Protein in complex with Zinc== | ||
<StructureSection load='3pvn' size='340' side='right' caption='[[3pvn]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='3pvn' size='340' side='right' caption='[[3pvn]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lj7|1lj7]], [[3pvo|3pvo]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lj7|1lj7]], [[3pvo|3pvo]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRP, PTX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRP, PTX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pvn RCSB], [http://www.ebi.ac.uk/pdbsum/3pvn PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvn OCA], [http://pdbe.org/3pvn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pvn RCSB], [http://www.ebi.ac.uk/pdbsum/3pvn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pvn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3pvn" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:54, 2 January 2017
Triclinic form of Human C-Reactive Protein in complex with ZincTriclinic form of Human C-Reactive Protein in complex with Zinc
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 PubMedHuman C-reactive protein (CRP) is an acute phase protein, which harbours both host defence and scavenging properties. In this study, we obtained two new crystal forms of CRP, where CRP forms a symmetric, staggered dimer of pentamers. In one of these structures, obtained in the presence of HIV-1 Tat protein, this dimer of pentamers is stabilized by two zinc ions trapped within a cleft of the effector face of CRP. These two decameric interfaces involve complementary surfaces of CRP pentamers and bury a large area of ~2000 A(2) per pentamer, suggesting a biological role of this interface. These two novel decameric interfaces and the involvement of zinc might have important consequences in the understanding of CRP biological functions. A Staggered Decameric Assembly of Human C-Reactive Protein Stabilized by Zinc Ions Revealed by X-ray Crystallography.,Guillon C, Bigouagou UM, Folio C, Jeannin P, Delneste Y, Gouet P Protein Pept Lett. 2014;22(3):248-55. PMID:25552313[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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