View source for 5dil


==Crystal structure of the effector domain of the NS1 protein from influenza virus B==
<StructureSection load='5dil' size='340' side='right'caption='[[5dil]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dil]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_B_virus_(B/Singapore/DSO_090134/2004) Influenza B virus (B/Singapore/DSO_090134/2004)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DIL 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]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5dil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dil OCA], [https://pdbe.org/5dil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dil RCSB], [https://www.ebi.ac.uk/pdbsum/5dil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dil ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/X2C382_9INFB X2C382_9INFB] Binds and inhibits the ubiquitin-like protein G1P2/ISG15, which is an early antiviral protein. Inhibits IRF-3 nuclear translocation and activation. Inhibits IFN-beta promoter activation; this inhibition is not dsRNA-binding dependent Prevents EIF2AK2/PKR activation, either by binding double strand RNA or by interacting directly with EIF2AK2/PKR. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells.[PIRNR:PIRNR003938]
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== Publication Abstract from PubMed ==
Influenza viruses cause a highly contagious respiratory disease in humans. The NS1 proteins of influenza A and B viruses (NS1A and NS1B proteins, respectively) are composed of two domains, a dimeric N-terminal domain and a C-terminal domain, connected by a flexible polypeptide linker. Here we report the 2.0-A X-ray crystal structure and nuclear magnetic resonance studies of the NS1B C-terminal domain, which reveal a novel and unexpected basic RNA-binding site that is not present in the NS1A protein. We demonstrate that single-site alanine replacements of basic residues in this site lead to reduced RNA-binding activity, and that recombinant influenza B viruses expressing these mutant NS1B proteins are severely attenuated in replication. This novel RNA-binding site of NS1B is required for optimal influenza B virus replication. Most importantly, this study reveals an unexpected RNA-binding function in the C-terminal domain of NS1B, a novel function that distinguishes influenza B viruses from influenza A viruses.

A Second RNA-Binding Site in the NS1 Protein of Influenza B Virus.,Ma LC, Guan R, Hamilton K, Aramini JM, Mao L, Wang S, Krug RM, Montelione GT Structure. 2016 Sep 6;24(9):1562-72. doi: 10.1016/j.str.2016.07.001. Epub 2016, Aug 18. PMID:27545620<ref>PMID:27545620</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 5dil" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Guan R]]
[[Category: Hamilton K]]
[[Category: Ma L]]
[[Category: Montelione GT]]