3vnf: Difference between revisions

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 ==Structure of the ebolavirus protein VP24 from Sudan==
-<StructureSection load='3vnf' size='340' side='right' caption='[[3vnf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='3vnf' size='340' side='right'caption='[[3vnf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3vnf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sudan_ebolavirus Sudan ebolavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VNF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3vnf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sudan_ebolavirus Sudan ebolavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VNF FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d9o|4d9o]], [[3vne|3vne]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP24 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186540 Sudan ebolavirus])</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=3vnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnf OCA], [https://pdbe.org/3vnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vnf RCSB], [https://www.ebi.ac.uk/pdbsum/3vnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vnf ProSAT]</span></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=3vnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vnf RCSB], [http://www.ebi.ac.uk/pdbsum/3vnf PDBsum]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/VP24_EBOSU VP24_EBOSU] Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. Blocks the IFN-induced nuclear accumulation of host phosphorylated STAT1, by interacting with the STAT1-binding region of host importin alpha-1/KPNA1 protein, thereby inhibiting the latter. Without the activity of this protein, activated STAT1 would not enter the nucleus and be unable to activate IFN-induced genes. Plays a role in assembly of viral nucleocapsid and virion budding. May act as a minor matrix protein that plays a role in assembly of viral nucleocapsid and virion budding.
-Ebolaviruses cause hemorrhagic fever with up to 90% lethality and in fatal cases, are characterized by early suppression of the host innate immune system. One of the proteins likely responsible for this effect is VP24. VP24 is known to antagonize interferon signaling by binding host karyopherin alpha proteins, thereby preventing them from transporting the tyrosine-phosphorylated transcription factor STAT1 to the nucleus. Here, we report that VP24 binds STAT1 directly, suggesting that VP24 can suppress at least two distinct branches of the interferon pathway. Here, we also report the first crystal structures of VP24, derived from different species of ebolavirus that are pathogenic (Sudan) and nonpathogenic to humans (Reston). These structures reveal that VP24 has a novel, pyramidal fold. A site on a particular face of the pyramid exhibits reduced solvent exchange when in complex with STAT1. This site is above two highly conserved pockets in VP24 that contain key residues previously implicated in virulence. These crystal structures and accompanying biochemical analysis map differences between pathogenic and nonpathogenic viruses, offer templates for drug design, and provide the three-dimensional framework necessary for biological dissection of the many functions of VP24 in the virus life cycle.
-The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold.,Zhang AP, Bornholdt ZA, Liu T, Abelson DM, Lee DE, Li S, Woods VL Jr, Saphire EO PLoS Pathog. 2012 Feb;8(2):e1002550. Epub 2012 Feb 23. PMID:22383882<ref>PMID:22383882</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
 *[[VP24|VP24]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Sudan ebolavirus]]
-[[Category: Zhang, A P.P]]
+[[Category: Zhang APP]]
-[[Category: Ebolavirus]]
-[[Category: Ifn response pathway]]
-[[Category: Interferon antagonist]]
-[[Category: Karyopherin alpha]]
-[[Category: Reston]]
-[[Category: Stat1]]
-[[Category: Sudan]]
-[[Category: Viral protein]]
-[[Category: Vp24]]
-[[Category: Vp35]]
-[[Category: Zaire]]