4ar2: Difference between revisions

← Older edit Newer edit →

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

OCA

@@ Line 1: / Line 1: @@
 ==Dodecahedron formed of penton base protein from adenovirus Ad3==
 <StructureSection load='4ar2' size='340' side='right' caption='[[4ar2]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ar2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_3 Human adenovirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AR2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ar2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade03 Ade03]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AR2 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>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qhv|1qhv]], [[1qiu|1qiu]], [[1v1h|1v1h]], [[1v1i|1v1i]], [[2c9f|2c9f]], [[4aqq|4aqq]]</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=4ar2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ar2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ar2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ar2 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=4ar2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ar2 OCA], [http://pdbe.org/4ar2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ar2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ar2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ar2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FIBP_ADE02 FIBP_ADE02]] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host coxsackievirus and adenovirus receptor CXADR located at the cell tight junctions to provide virion initial attachment to target cell. The fiber protein binds to CXADR with a higher affinity than CXADR binds to itself, thereby blocking the cell-cell adhesion function of CXADR dimers and leading to local disruption of the tight junction. Fiber protein present on neo-synthesized particles may thus disrupt the junctional integrity in order to facilitate further neighboring cells infection. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Fiber shedding is dependent on viral CXADR drifting motion and subsequent binding to immobile integrins. Heparan sulfate might also play a role in virus binding.<ref>PMID:9525681</ref> <ref>PMID:10704346</ref> <ref>PMID:12297051</ref> <ref>PMID:21843868</ref>
+[[http://www.uniprot.org/uniprot/SPIKE_ADE02 SPIKE_ADE02]] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host coxsackievirus and adenovirus receptor CXADR located at the cell tight junctions to provide virion initial attachment to target cell. The fiber protein binds to CXADR with a higher affinity than CXADR binds to itself, thereby blocking the cell-cell adhesion function of CXADR dimers and leading to local disruption of the tight junction. Fiber protein present on neo-synthesized particles may thus disrupt the junctional integrity in order to facilitate further neighboring cells infection. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Fiber shedding is dependent on viral CXADR drifting motion and subsequent binding to immobile integrins. Heparan sulfate might also play a role in virus binding.<ref>PMID:10704346</ref> <ref>PMID:12297051</ref> <ref>PMID:21843868</ref> <ref>PMID:9525681</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ar2" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human adenovirus 3]]
+[[Category: Ade03]]
 [[Category: Andreev, I]]
 [[Category: Andrieu, J P]]