3pvo: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Monoclinic form of Human C-Reactive Protein==
-<StructureSection load='3pvo' size='340' side='right' caption='[[3pvo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='3pvo' size='340' side='right'caption='[[3pvo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3pvo]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PVO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3pvo]] 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=3PVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PVO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pvn|3pvn]], [[1lj7|1lj7]]</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></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 Homo sapiens])</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=3pvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvo OCA], [https://pdbe.org/3pvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pvo RCSB], [https://www.ebi.ac.uk/pdbsum/3pvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pvo ProSAT]</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=3pvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pvo RCSB], [http://www.ebi.ac.uk/pdbsum/3pvo PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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;">
+== Publication Abstract from PubMed ==
+Human 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<ref>PMID:25552313</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3pvo" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[C-reactive protein|C-reactive protein]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Bigouagou, U Mavoungou]]
+[[Category: Large Structures]]
-[[Category: Delneste, Y]]
+[[Category: Delneste Y]]
-[[Category: Gouet, P]]
+[[Category: Gouet P]]
-[[Category: Guillon, C]]
+[[Category: Guillon C]]
-[[Category: Jeannin, P]]
+[[Category: Jeannin P]]
-[[Category: Immune system]]
+[[Category: Mavoungou Bigouagou U]]
-[[Category: Pentraxin family]]