6oaf

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Current revision (07:06, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6oaf' size='340' side='right'caption='[[6oaf]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6oaf' size='340' side='right'caption='[[6oaf]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6oaf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ebosb Ebosb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OAF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6oaf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sudan_ebolavirus_-_Uganda_(2000) Sudan ebolavirus - Uganda (2000)] and [https://en.wikipedia.org/wiki/Sudan_virus_-_Boniface,_Sudan,1976 Sudan virus - Boniface, Sudan,1976]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OAF FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=128948 EBOSB])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=6oaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oaf OCA], [http://pdbe.org/6oaf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oaf RCSB], [http://www.ebi.ac.uk/pdbsum/6oaf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oaf ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6oaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oaf OCA], [https://pdbe.org/6oaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oaf RCSB], [https://www.ebi.ac.uk/pdbsum/6oaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oaf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VP35_EBOSU VP35_EBOSU]] 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. This blockage is produced through the interaction with and inhibition host IKBKE and TBK1 producing a strong inhibition of the phosphorylation and activation of IRF3. Also inhibits the antiviral effect mediated by the interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR (By similarity).
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[https://www.uniprot.org/uniprot/NCAP_EBOSB NCAP_EBOSB] Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response. VP35 binds to and stabilizes monomeric NP, keeping it soluble. Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm. Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid. Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription. Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1.[UniProtKB:P18272][https://www.uniprot.org/uniprot/VP35_EBOSU VP35_EBOSU] 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. This blockage is produced through the interaction with and inhibition host IKBKE and TBK1 producing a strong inhibition of the phosphorylation and activation of IRF3. 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>
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[[Category: Ebosb]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Landeras-Bueno, S]]
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[[Category: Sudan virus - Boniface, Sudan,1976]]
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[[Category: Norris, M J]]
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[[Category: Landeras-Bueno S]]
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[[Category: Oda, S]]
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[[Category: Li Salie Z]]
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[[Category: Salie, Z Li]]
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[[Category: Norris MJ]]
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[[Category: Saphire, E Ollmann]]
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[[Category: Oda S]]
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[[Category: Complex sudv np-vp35]]
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[[Category: Ollmann Saphire E]]
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[[Category: Viral protein]]
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Current revision

Sudan virus nucleoprotein core domain in complex with VP35 chaperoning peptide

PDB ID 6oaf

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