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[[Image:1ns1.png|left|200px]]


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==RNA-BINDING DOMAIN OF NON-STRUCTURAL PROTEIN 1 FROM INFLUENZA VIRUS, NMR, 16 STRUCTURES==
The line below this paragraph, containing "STRUCTURE_1ns1", creates the "Structure Box" on the page.
<StructureSection load='1ns1' size='340' side='right'caption='[[1ns1]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ns1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NS1 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ns1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ns1 OCA], [https://pdbe.org/1ns1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ns1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ns1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ns1 ProSAT]</span></td></tr>
{{STRUCTURE_1ns1|  PDB=1ns1  |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/NS1_I72A2 NS1_I72A2] 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.<ref>PMID:9651582</ref> <ref>PMID:9560194</ref> <ref>PMID:16571812</ref>  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).<ref>PMID:9651582</ref> <ref>PMID:9560194</ref> <ref>PMID:16571812</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution NMR structure of the RNA-binding domain from influenza virus non-structural protein 1 exhibits a novel dimeric six-helical protein fold. Distributions of basic residues and conserved salt bridges of dimeric NS1(1-73) suggest that the face containing antiparallel helices 2 and 2' forms a novel arginine-rich nucleic acid binding motif.


===RNA-BINDING DOMAIN OF NON-STRUCTURAL PROTEIN 1 FROM INFLUENZA VIRUS, NMR, 16 STRUCTURES===
A novel RNA-binding motif in influenza A virus non-structural protein 1.,Chien CY, Tejero R, Huang Y, Zimmerman DE, Rios CB, Krug RM, Montelione GT Nat Struct Biol. 1997 Nov;4(11):891-5. PMID:9360601<ref>PMID:9360601</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ns1" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]]
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== References ==
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<references/>
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</StructureSection>
==About this Structure==
[[Category: Influenza A virus]]
1NS1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NS1 OCA].
[[Category: Large Structures]]
 
[[Category: Chien C-Y]]
==Reference==
[[Category: Montelione GT]]
A novel RNA-binding motif in influenza A virus non-structural protein 1., Chien CY, Tejero R, Huang Y, Zimmerman DE, Rios CB, Krug RM, Montelione GT, Nat Struct Biol. 1997 Nov;4(11):891-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9360601 9360601]
[[Category: Tejero R]]
[[Category: Influenza a virus]]
[[Category: Single protein]]
[[Category: Chien, C Y.]]
[[Category: Montelione, G T.]]
[[Category: Tejero, R.]]
[[Category: Dimeric six helical structure]]
[[Category: Dsrna-binding]]
[[Category: Nonstructural protein]]
[[Category: Polya-rna-binding]]
[[Category: Rna-binding]]
[[Category: Ssrna-binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:17:04 2008''

Latest revision as of 21:53, 29 November 2023

RNA-BINDING DOMAIN OF NON-STRUCTURAL PROTEIN 1 FROM INFLUENZA VIRUS, NMR, 16 STRUCTURESRNA-BINDING DOMAIN OF NON-STRUCTURAL PROTEIN 1 FROM INFLUENZA VIRUS, NMR, 16 STRUCTURES

Structural highlights

1ns1 is a 2 chain structure with sequence from Influenza A virus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NS1_I72A2 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.[1] [2] [3] 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).[4] [5] [6]

Publication Abstract from PubMed

The solution NMR structure of the RNA-binding domain from influenza virus non-structural protein 1 exhibits a novel dimeric six-helical protein fold. Distributions of basic residues and conserved salt bridges of dimeric NS1(1-73) suggest that the face containing antiparallel helices 2 and 2' forms a novel arginine-rich nucleic acid binding motif.

A novel RNA-binding motif in influenza A virus non-structural protein 1.,Chien CY, Tejero R, Huang Y, Zimmerman DE, Rios CB, Krug RM, Montelione GT Nat Struct Biol. 1997 Nov;4(11):891-5. PMID:9360601[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM. Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs. Mol Cell. 1998 Jun;1(7):991-1000. PMID:9651582
  2. ↑ Li Y, Yamakita Y, Krug RM. Regulation of a nuclear export signal by an adjacent inhibitory sequence: the effector domain of the influenza virus NS1 protein. Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4864-9. PMID:9560194
  3. ↑ Twu KY, Noah DL, Rao P, Kuo RL, Krug RM. The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target. J Virol. 2006 Apr;80(8):3957-65. PMID:16571812 doi:10.1128/JVI.80.8.3957-3965.2006
  4. ↑ Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM. Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs. Mol Cell. 1998 Jun;1(7):991-1000. PMID:9651582
  5. ↑ Li Y, Yamakita Y, Krug RM. Regulation of a nuclear export signal by an adjacent inhibitory sequence: the effector domain of the influenza virus NS1 protein. Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4864-9. PMID:9560194
  6. ↑ Twu KY, Noah DL, Rao P, Kuo RL, Krug RM. The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target. J Virol. 2006 Apr;80(8):3957-65. PMID:16571812 doi:10.1128/JVI.80.8.3957-3965.2006
  7. ↑ Chien CY, Tejero R, Huang Y, Zimmerman DE, Rios CB, Krug RM, Montelione GT. A novel RNA-binding motif in influenza A virus non-structural protein 1. Nat Struct Biol. 1997 Nov;4(11):891-5. PMID:9360601
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