View source for 1ns1

==RNA-BINDING DOMAIN OF NON-STRUCTURAL PROTEIN 1 FROM INFLUENZA VIRUS, NMR, 16 STRUCTURES==
<StructureSection load='1ns1' size='340' side='right' caption='[[1ns1]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ns1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/9infa 9infa]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NS1 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">J02169 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11320 9INFA])</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=1ns1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ns1 OCA], [http://pdbe.org/1ns1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ns1 RCSB], [http://www.ebi.ac.uk/pdbsum/1ns1 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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>  
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== 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<ref>PMID:9360601</ref>

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

==See Also==
*[[Nonstructural protein|Nonstructural protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[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]]