View source for 6dku


==Crystal structure of Myotis VP35 mutant of interferon inhibitory domain==
<StructureSection load='6dku' size='340' side='right'caption='[[6dku]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6dku]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myotis_lucifugus Myotis lucifugus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DKU 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]] 2.6&#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=6dku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dku OCA], [https://pdbe.org/6dku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dku RCSB], [https://www.ebi.ac.uk/pdbsum/6dku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dku ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G9JKD1_MYOLU G9JKD1_MYOLU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Non-retroviral integrated RNA viral sequences (NIRVs) potentially encoding approximately 280 amino acid homologs to filovirus VP35 proteins are present across the Myotis genus of bats. These are estimated to have been maintained for approximately 18 million years, indicating their co-option. To address the reasons for co-option, 16 Myotis VP35s were characterized in comparison to VP35s from the extant filoviruses Ebola virus and Marburg virus, in which VP35s play critical roles in immune evasion and RNA synthesis. The Myotis VP35s demonstrated a conserved suppression of innate immune signaling, albeit with reduced potency, in either human or Myotis cells. Their attenuation reflects a lack of dsRNA binding that in the filoviral VP35s correlates with potent suppression of interferon responses. Despite divergent function, evolution has preserved in Myotis the structure of the filoviral VP35s, indicating that this structure is critical for co-opted function, possibly as a regulator of innate immune signaling.

Conservation of Structure and Immune Antagonist Functions of Filoviral VP35 Homologs Present in Microbat Genomes.,Edwards MR, Liu H, Shabman RS, Ginell GM, Luthra P, Ramanan P, Keefe LJ, Kollner B, Amarasinghe GK, Taylor DJ, Leung DW, Basler CF Cell Rep. 2018 Jul 24;24(4):861-872.e6. doi: 10.1016/j.celrep.2018.06.045. PMID:30044983<ref>PMID:30044983</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Myotis lucifugus]]
[[Category: Amarasinghe GK]]
[[Category: Ginell GM]]
[[Category: Keefe LJ]]
[[Category: Leung DW]]
[[Category: Liu H]]