View source for 6gbq


==Crystal Structure of the oligomerization domain of Vp35 from Reston virus==
<StructureSection load='6gbq' size='340' side='right' caption='[[6gbq]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gbq]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ebola_virus_reston Ebola virus reston]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GBQ FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP35, REBOVgp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186539 Ebola virus Reston])</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=6gbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gbq OCA], [http://pdbe.org/6gbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gbq RCSB], [http://www.ebi.ac.uk/pdbsum/6gbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gbq ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/VP35_EBORR VP35_EBORR]] Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex. Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factor 3 (IRF3), a transcription factor critical for the induction of interferons alpha and beta. The mechanism by which this blockage occurs remains incompletely defined, a hypothesis suggests that VP35 dsRNA-binding activity prevents activation of IRF3 by sequestering dsRNA. Also inhibits the antiviral effect mediated by the interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR (By similarity). 
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== Publication Abstract from PubMed ==
The multifunctional virion protein 35 (VP35) of ebolaviruses is a critical determinant of virulence and pathogenesis indispensable for viral replication and host innate immune evasion. Essential for VP35 function is homo-oligomerization via a coiled-coil motif. Here we report crystal structures of VP35 oligomerization domains from the prototypic Ebola virus (EBOV) and the non-pathogenic Reston virus (RESTV), together with a comparative biophysical characterization of the domains from all known species of the Ebolavirus genus. EBOV and RESTV VP35 oligomerization domains form bipartite parallel helix bundles with a canonical coiled coil in the N-terminal half and increased plasticity in the highly conserved C-terminal half. The domain assembles into trimers and tetramers in EBOV, whereas it exclusively forms tetramers in all other ebolavirus species. Substitution of coiled-coil leucine residues critical for immune antagonism leads to aberrant oligomerization. A conserved arginine involved in inter-chain salt bridges stabilizes the VP35 oligomerization domain and modulates between coiled-coil oligomeric states.

Structures of Ebola and Reston Virus VP35 Oligomerization Domains and Comparative Biophysical Characterization in All Ebolavirus Species.,Zinzula L, Nagy I, Orsini M, Weyher-Stingl E, Bracher A, Baumeister W Structure. 2018 Oct 5. pii: S0969-2126(18)30335-6. doi:, 10.1016/j.str.2018.09.009. PMID:30482729<ref>PMID:30482729</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ebola virus reston]]
[[Category: Baumeister, W]]
[[Category: Bracher, A]]
[[Category: Nagy, I]]
[[Category: Orsini, M]]
[[Category: Weyher-Stingl, E]]
[[Category: Zinzula, L]]
[[Category: Coiled-coil]]
[[Category: Viral protein]]