3o9r: Difference between revisions
New page: '''Unreleased structure''' The entry 3o9r is ON HOLD Authors: Kerry, P.S., Lewis, A., Hale, B.G., Hass, C., Taylor, M.A., Randall, R.E., Russell, R.J.M. Description: Effector domain of... |
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==Effector domain of NS1 from influenza A/PR/8/34 containing a W187A mutation== | |||
<StructureSection load='3o9r' size='340' side='right'caption='[[3o9r]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3o9r]] 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=3O9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O9R FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=3o9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o9r OCA], [https://pdbe.org/3o9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o9r RCSB], [https://www.ebi.ac.uk/pdbsum/3o9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o9r ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NS1_I34A1 NS1_I34A1] 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). 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). | |||
==See Also== | |||
*[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Hale BG]] | |||
[[Category: Hass C]] | |||
[[Category: Kerry PS]] | |||
[[Category: Lewis A]] | |||
[[Category: Randall RE]] | |||
[[Category: Russell RJM]] | |||
[[Category: Taylor MA]] | |||
Latest revision as of 13:04, 14 February 2024
Effector domain of NS1 from influenza A/PR/8/34 containing a W187A mutationEffector domain of NS1 from influenza A/PR/8/34 containing a W187A mutation
Structural highlights
FunctionNS1_I34A1 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). 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). See Also |
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