1v1i: Difference between revisions

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<StructureSection load='1v1i' size='340' side='right'caption='[[1v1i]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1v1i' size='340' side='right'caption='[[1v1i]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1v1i]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Ade02 Ade02]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V1I FirstGlance]. <br>
<table><tr><td colspan='2'>[[1v1i]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Human_mastadenovirus_C Human mastadenovirus C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V1I FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aa0|1aa0]], [[1avy|1avy]], [[1ox3|1ox3]], [[1rfo|1rfo]], [[1qiu|1qiu]], [[1v1h|1v1h]]</div></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]] 1.9&#8491;</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=1v1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v1i OCA], [https://pdbe.org/1v1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v1i RCSB], [https://www.ebi.ac.uk/pdbsum/1v1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v1i ProSAT]</span></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=1v1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v1i OCA], [https://pdbe.org/1v1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v1i RCSB], [https://www.ebi.ac.uk/pdbsum/1v1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v1i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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>
[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').[https://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>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ade02]]
[[Category: Escherichia virus T4]]
[[Category: Human mastadenovirus C]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Belrhali, H]]
[[Category: Belrhali H]]
[[Category: Forsyth, V T]]
[[Category: Forsyth VT]]
[[Category: Mitraki, A]]
[[Category: Mitraki A]]
[[Category: Papanikolopoulou, K]]
[[Category: Papanikolopoulou K]]
[[Category: Raaij, M J.van]]
[[Category: Teixeira S]]
[[Category: Teixeira, S]]
[[Category: Van Raaij MJ]]
[[Category: Adenovirus]]
[[Category: Chimera]]
[[Category: Fiber protein]]

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