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2of6
From Proteopedia
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| - | [[Image:2of6.gif|left|200px]]<br /><applet load="2of6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2of6" /> | ||
| - | '''Structure of immature West Nile virus'''<br /> | ||
| - | == | + | ==Structure of immature West Nile virus== |
| + | <SX load='2of6' size='340' side='right' viewer='molstar' caption='[[2of6]], [[Resolution|resolution]] 24.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2of6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/West_Nile_virus West Nile virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OF6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 24Å</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=2of6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2of6 OCA], [https://pdbe.org/2of6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2of6 RCSB], [https://www.ebi.ac.uk/pdbsum/2of6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2of6 ProSAT]</span></td></tr> | ||
| + | </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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The structure of immature West Nile virus particles, propagated in the presence of ammonium chloride to block virus maturation in the low-pH environment of the trans-Golgi network, was determined by cryo-electron microscopy (cryo-EM). The structure of these particles was similar to that of immature West Nile virus particles found as a minor component of mature virus samples (naturally occurring immature particles [NOIPs]). The structures of mature infectious flaviviruses are radically different from those of the immature particles. The similarity of the ammonium chloride-treated particles and NOIPs suggests either that the NOIPs have not undergone any conformational change during maturation or that the conformational change is reversible. Comparison with the cryo-EM reconstruction of immature dengue virus established the locations of the N-linked glycosylation sites of these viruses, verifying the interpretation of the reconstructions of the immature flaviviruses. | The structure of immature West Nile virus particles, propagated in the presence of ammonium chloride to block virus maturation in the low-pH environment of the trans-Golgi network, was determined by cryo-electron microscopy (cryo-EM). The structure of these particles was similar to that of immature West Nile virus particles found as a minor component of mature virus samples (naturally occurring immature particles [NOIPs]). The structures of mature infectious flaviviruses are radically different from those of the immature particles. The similarity of the ammonium chloride-treated particles and NOIPs suggests either that the NOIPs have not undergone any conformational change during maturation or that the conformational change is reversible. Comparison with the cryo-EM reconstruction of immature dengue virus established the locations of the N-linked glycosylation sites of these viruses, verifying the interpretation of the reconstructions of the immature flaviviruses. | ||
| - | + | Structure of immature West Nile virus.,Zhang Y, Kaufmann B, Chipman PR, Kuhn RJ, Rossmann MG J Virol. 2007 Jun;81(11):6141-5. Epub 2007 Mar 21. PMID:17376919<ref>PMID:17376919</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2of6" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: West Nile virus]] | ||
| + | [[Category: Chipman PR]] | ||
| + | [[Category: Kaufmann B]] | ||
| + | [[Category: Kuhn RJ]] | ||
| + | [[Category: Rossmann MG]] | ||
| + | [[Category: Zhang Y]] | ||
Current revision
Structure of immature West Nile virus
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