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4lg2
From Proteopedia
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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 [ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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='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). |
<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: | + | [[Category: Large Structures]] |
| - | [[Category: Bale | + | [[Category: Bale S]] |
| - | [[Category: Bornholdt | + | [[Category: Bornholdt ZA]] |
| - | + | [[Category: Julien J-P]] | |
| - | [[Category: Julien | + | [[Category: Krois AS]] |
| - | [[Category: Krois | + | [[Category: Saphire EO]] |
| - | [[Category: | + | [[Category: Wilson IA]] |
| - | [[Category: | + | |
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Current revision
Crystal structure of Reston Ebola virus VP35 RNA binding domain bound to 12-bp dsRNA
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