2fp7: Difference between revisions

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-{{Seed}}
-[[Image:2fp7.png|left|200px]]
-<!--
+==West Nile Virus NS2B/NS3protease in complex with Bz-Nle-Lys-Arg-Arg-H==
-The line below this paragraph, containing "STRUCTURE_2fp7", creates the "Structure Box" on the page.
+<StructureSection load='2fp7' size='340' side='right'caption='[[2fp7]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2fp7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/West_Nile_virus West Nile virus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FP7 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=OAR:N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE'>OAR</scene></td></tr>
-{{STRUCTURE_2fp7|  PDB=2fp7  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fp7 OCA], [https://pdbe.org/2fp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fp7 RCSB], [https://www.ebi.ac.uk/pdbsum/2fp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fp7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/POLG_WNV POLG_WNV] 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:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</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:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</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:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</ref>   Non-structural protein 1 is involved in virus replication and regulation of the innate immune response (By similarity).<ref>PMID:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</ref>   Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential).<ref>PMID:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</ref>   Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity).<ref>PMID:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</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:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</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:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</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:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</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:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</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 (By similarity).<ref>PMID:15367621</ref> <ref>PMID:15956546</ref> <ref>PMID:17267492</ref> <ref>PMID:20106931</ref> <ref>PMID:19850911</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/fp/2fp7_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=2fp7 ConSurf].
+<div style="clear:both"></div>
-===West Nile Virus NS2B/NS3protease in complex with Bz-Nle-Lys-Arg-Arg-H===
+==See Also==
+*[[Virus protease 3D structures|Virus protease 3D structures]]
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_16532006}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 16532006 is the PubMed ID number.
+</StructureSection>
--->
+[[Category: Large Structures]]
-{{ABSTRACT_PUBMED_16532006}}
+[[Category: Synthetic construct]]
+[[Category: West Nile virus]]
-==About this Structure==
+[[Category: D'Arcy A]]
-FP7 is a [[Protein complex]] structure of sequences from [http://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=2FP7 OCA].
+[[Category: Erbel P]]
+[[Category: Schiering N]]
-==Reference==
-Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus., Erbel P, Schiering N, D'Arcy A, Renatus M, Kroemer M, Lim SP, Yin Z, Keller TH, Vasudevan SG, Hommel U, Nat Struct Mol Biol. 2006 Apr;13(4):372-3. Epub 2006 Mar 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16532006 16532006]
-[[Category: Flavivirin]]
-[[Category: Protein complex]]
-[[Category: West nile virus]]
-[[Category: Arcy, A D.]]
-[[Category: Erbel, P.]]
-[[Category: Schiering, N.]]
-[[Category: Flavivirus]]
-[[Category: Ns2b cofactor]]
-[[Category: Ns3 protease]]
-[[Category: Substrate-based inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:46:01 2008''