3ks8
From Proteopedia
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==Crystal structure of Reston ebolavirus VP35 RNA binding domain in complex with 18bp dsRNA== | ==Crystal structure of Reston ebolavirus VP35 RNA binding domain in complex with 18bp dsRNA== | ||
- | <StructureSection load='3ks8' size='340' side='right' caption='[[3ks8]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='3ks8' size='340' side='right'caption='[[3ks8]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3ks8]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3ks8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Reston_ebolavirus_-_Reston Reston ebolavirus - Reston]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KS8 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.401Å</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=3ks8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ks8 OCA], [https://pdbe.org/3ks8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ks8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ks8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ks8 ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [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). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/3ks8_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/3ks8_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
- | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ks8 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 3ks8" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Reston ebolavirus]] | + | [[Category: Large Structures]] |
- | [[Category: Bornholdt | + | [[Category: Reston ebolavirus - Reston]] |
- | [[Category: Kimberlin | + | [[Category: Bornholdt ZA]] |
- | [[Category: Li | + | [[Category: Kimberlin CR]] |
- | [[Category: Macrae | + | [[Category: Li S]] |
- | [[Category: Saphire | + | [[Category: Macrae IJ]] |
- | [[Category: Woods | + | [[Category: Saphire EO]] |
- | + | [[Category: Woods VL]] | |
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Current revision
Crystal structure of Reston ebolavirus VP35 RNA binding domain in complex with 18bp dsRNA
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