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| | ==Crystal structure of Reston Ebola virus VP35 RNA binding domain bound to 12-bp dsRNA== | | ==Crystal structure of Reston Ebola virus VP35 RNA binding domain bound to 12-bp dsRNA== |
| - | <StructureSection load='4lg2' size='340' side='right' caption='[[4lg2]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4lg2' size='340' side='right'caption='[[4lg2]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lg2]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Eborr Eborr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LG2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lg2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Reston_ebolavirus_-_Reston_(1989) Reston ebolavirus - Reston (1989)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LG2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ks8|3ks8]], [[3fke|3fke]], [[3l25|3l25]], [[4gha|4gha]], [[3l26|3l26]]</td></tr> | + | </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=4lg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lg2 OCA], [https://pdbe.org/4lg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lg2 RCSB], [https://www.ebi.ac.uk/pdbsum/4lg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lg2 ProSAT]</span></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=386032 EBORR])</td></tr>
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| - | <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=4lg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lg2 OCA], [http://pdbe.org/4lg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4lg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lg2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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). | + | [https://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). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eborr]] | + | [[Category: Large Structures]] |
| - | [[Category: Bale, S]] | + | [[Category: Bale S]] |
| - | [[Category: Bornholdt, Z A]] | + | [[Category: Bornholdt ZA]] |
| - | [[Category: Julien, J P]] | + | [[Category: Julien J-P]] |
| - | [[Category: Krois, A S]] | + | [[Category: Krois AS]] |
| - | [[Category: Saphire, E O]] | + | [[Category: Saphire EO]] |
| - | [[Category: Wilson, I A]] | + | [[Category: Wilson IA]] |
| - | [[Category: Dsrna]]
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| - | [[Category: Dsrna binding protein]]
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| - | [[Category: Rna binding domain]]
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| - | [[Category: Rna binding protein-rna complex]]
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| Structural highlights
Function
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).
Publication Abstract from PubMed
Recognition of viral double-stranded RNA (dsRNA) activates interferon production and immune signaling in host cells. Crystal structures of ebolavirus VP35 show that it caps dsRNA ends to prevent sensing by pattern recognition receptors such as RIG-I. By contrast, structures of marburgvirus VP35 show that it primarily coats the dsRNA backbone. Here, we demonstrate that ebolavirus VP35 also coats the dsRNA backbone in solution, although binding to the dsRNA ends probably constitutes the initial binding event.
Ebolavirus VP35 also coats the backbone of dsRNA for interferon antagonism.,Bale S, Julien JP, Bornholdt ZA, Krois AS, Wilson IA, Saphire EO J Virol. 2013 Jul 3. PMID:23824825[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bale S, Julien JP, Bornholdt ZA, Krois AS, Wilson IA, Saphire EO. Ebolavirus VP35 also coats the backbone of dsRNA for interferon antagonism. J Virol. 2013 Jul 3. PMID:23824825 doi:10.1128/JVI.01452-13
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