3m5r

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Current revision (08:48, 6 September 2023) (edit) (undo)
 
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<StructureSection load='3m5r' size='340' side='right'caption='[[3m5r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3m5r' size='340' side='right'caption='[[3m5r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3m5r]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_a_virus_(a/california/07/2009(h1n1)) Influenza a virus (a/california/07/2009(h1n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M5R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3m5r]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/California/07/2009(H1N1)) Influenza A virus (A/California/07/2009(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M5R FirstGlance]. <br>
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</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=641809 Influenza A virus (A/California/07/2009(H1N1))])</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&#8491;</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=3m5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5r OCA], [https://pdbe.org/3m5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m5r RCSB], [https://www.ebi.ac.uk/pdbsum/3m5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m5r 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=3m5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5r OCA], [https://pdbe.org/3m5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m5r RCSB], [https://www.ebi.ac.uk/pdbsum/3m5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m5r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/D2Y6Z6_9INFA D2Y6Z6_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.[SAAS:SAAS00141143] 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.[SAAS:SAAS00141179]
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[https://www.uniprot.org/uniprot/C3W611_9INFA C3W611_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.[SAAS:SAAS00141143] 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.[SAAS:SAAS00141179]
==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Fremont DH]]
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[[Category: Fremont, D H]]
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[[Category: Nelson CA]]
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[[Category: Nelson, C A]]
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[[Category: Yu YYL]]
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[[Category: Yu, Y Y.L]]
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[[Category: Csgid]]
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[[Category: Effector domain]]
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[[Category: Influenza a h1n1 subtype]]
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[[Category: Niaid]]
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[[Category: Nonstructural protein 1]]
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[[Category: Swine flu virus]]
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[[Category: Viral immune evasion]]
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[[Category: Viral protein]]
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Current revision

Crystal Structure of Swine Flu Virus NS1 Effector Domain from H1N1 Influenza A/California/07/2009

PDB ID 3m5r

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