2hcs: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HCS FirstGlance]. <br> | <table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HCS FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hcn|2hcn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hcn|2hcn]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hcs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hcs RCSB], [http://www.ebi.ac.uk/pdbsum/2hcs PDBsum]</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=2hcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hcs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hcs RCSB], [http://www.ebi.ac.uk/pdbsum/2hcs PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Kunjin virus]] | [[Category: Kunjin virus]] | ||
[[Category: RNA-directed RNA polymerase]] | [[Category: RNA-directed RNA polymerase]] | ||
[[Category: Egloff, M P | [[Category: Egloff, M P]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Malet, H | [[Category: Malet, H]] | ||
[[Category: Msgp]] | [[Category: Msgp]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Viral enzymes involved in replication]] | [[Category: Viral enzymes involved in replication]] | ||
[[Category: Vizier]] | [[Category: Vizier]] | ||
[[Category: West-nile virus rna polymerase]] | [[Category: West-nile virus rna polymerase]] | ||