3o9t: Difference between revisions

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==Effector domain from influenza A/PR/8/34 NS1==
==Effector domain from influenza A/PR/8/34 NS1==
<StructureSection load='3o9t' size='340' side='right' caption='[[3o9t]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3o9t' size='340' side='right'caption='[[3o9t]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o9t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/reassortant/ivr108(sydney/5/1995_x_puerto_rico/8/1934)(h3n2)) Influenza a virus (a/reassortant/ivr108(sydney/5/1995 x puerto rico/8/1934)(h3n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O9T FirstGlance]. <br>
<table><tr><td colspan='2'>[[3o9t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_a_virus_(a/reassortant/ivr108(sydney/5/1995_x_puerto_rico/8/1934)(h3n2)) Influenza a virus (a/reassortant/ivr108(sydney/5/1995 x puerto rico/8/1934)(h3n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O9T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o9q|3o9q]], [[3o9r|3o9r]], [[3o9s|3o9s]], [[3o9u|3o9u]], [[3oa9|3oa9]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3o9q|3o9q]], [[3o9r|3o9r]], [[3o9s|3o9s]], [[3o9u|3o9u]], [[3oa9|3oa9]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=671829 Influenza A virus (A/reassortant/IVR108(Sydney/5/1995 x Puerto Rico/8/1934)(H3N2))])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=671829 Influenza A virus (A/reassortant/IVR108(Sydney/5/1995 x Puerto Rico/8/1934)(H3N2))])</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=3o9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o9t OCA], [http://pdbe.org/3o9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o9t RCSB], [http://www.ebi.ac.uk/pdbsum/3o9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o9t ProSAT]</span></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=3o9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o9t OCA], [https://pdbe.org/3o9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o9t RCSB], [https://www.ebi.ac.uk/pdbsum/3o9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o9t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/C9S2D8_9INFA C9S2D8_9INFA]] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity).[SAAS:SAAS00210185]  Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity).[SAAS:SAAS00210196]  
[[https://www.uniprot.org/uniprot/C9S2D8_9INFA C9S2D8_9INFA]] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity).[SAAS:SAAS00210185]  Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity).[SAAS:SAAS00210196]  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Nonstructural protein|Nonstructural protein]]
*[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Hale, B G]]
[[Category: Hale, B G]]
[[Category: Hass, C]]
[[Category: Hass, C]]

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