2hcs: Difference between revisions

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-[[Image:2hcs.png|left|200px]]
-{{STRUCTURE_2hcs|  PDB=2hcs  |  SCENE=  }}
+==Crystal structure of RNA dependant RNA polymerase domain of West Nile virus==
+<StructureSection load='2hcs' size='340' side='right'caption='[[2hcs]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-===Crystal structure of RNA dependant RNA polymerase domain of West Nile virus===
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2hcs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kunjin_virus Kunjin virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HCS FirstGlance]. <br>
-{{ABSTRACT_PUBMED_17287213}}
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-==About this Structure==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hcs OCA], [https://pdbe.org/2hcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hcs RCSB], [https://www.ebi.ac.uk/pdbsum/2hcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hcs ProSAT]</span></td></tr>
-[[2hcs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Kunjin_virus Kunjin virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HCS OCA].
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/POLG_KUNJM POLG_KUNJM] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   Non-structural protein 1 is involved in virus replication and regulation of the innate immune response (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway (By similarity).<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>   RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.<ref>PMID:18337583</ref> <ref>PMID:20686019</ref> <ref>PMID:15650160</ref> <ref>PMID:20106931</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/2hcs_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hcs ConSurf].
+<div style="clear:both"></div>
 ==See Also==
-*[[RNA polymerase|RNA polymerase]]
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:017287213</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Kunjin virus]]
-[[Category: RNA-directed RNA polymerase]]
+[[Category: Large Structures]]
-[[Category: Egloff, M P.]]
+[[Category: Egloff MP]]
-[[Category: MSGP, Marseilles Structural Genomics Program.@.AFMB.]]
+[[Category: Malet H]]
-[[Category: Malet, H.]]
-[[Category: Marseilles structural genomics program @ afmb]]
-[[Category: Msgp]]
-[[Category: Structural genomic]]
-[[Category: Transferase]]
-[[Category: Viral enzymes involved in replication]]
-[[Category: Vizier]]
-[[Category: West-nile virus rna polymerase]]