2gg1 - Revision history

OCA at 14:18, 29 November 2023

2023-11-29T14:18:44Z

←Older revision		Revision as of 14:18, 29 November 2023
Line 1:		Line 1:

	==NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)==		==NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)==
-	<StructureSection load='2gg1' size='340' side='right'caption='[[2gg1~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2gg1' size='340' side='right'caption='[[2gg1]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Flavivirus_langat Flavivirus langat~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Langat_virus Langat virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[1z66\|1z66]]</div~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [https://pdbe.org/2gg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2gg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gg1 ProSAT]</span></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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [https://pdbe.org/2gg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2gg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gg1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~POLG_LANVY POLG_LANVY~~]~~] Capsid protein C self-assembles~~ to ~~form an icosahedral capsid about 30 nm~~ in ~~diameter~~. ~~The capsid encapsulates~~ the ~~genomic~~ RNA ~~(By similarity)~~. ~~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)~~. ~~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).	+	[https://www.uniprot.org/uniprot/POLG_LANVT POLG_LANVT] Plays a role in virus budding by binding to membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration in host cytoplasm after hemifusion induced by surface proteins. Can migrate to the cell nucleus where it modulates host functions.[UniProtKB:P17763] Inhibits RNA silencing by interfering with host Dicer.[UniProtKB:P03314] Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space gets dissociated from E dimers.[UniProtKB:P17763] Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network. Presumably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.[UniProtKB:P17763] May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M extodomain. May display a viroporin activity.[UniProtKB:P17763] Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.[UniProtKB:P17763] Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).[UniProtKB:Q9Q6P4] Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.[UniProtKB:P17763] Required cofactor for the serine protease function of NS3 (By similarity). May have membrane-destabilizing activity and form viroporins (By similarity).[UniProtKB:P17763][PROSITE-ProRule:PRU00859] 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.[PROSITE-ProRule:PRU00860] Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.[UniProtKB:Q9Q6P4] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[UniProtKB:P17763] Induces the formation of ER-derived membrane vesicles where the viral replication takes place. 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. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.[UniProtKB:Q9Q6P4] Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). 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 (PubMed:16188985). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:16188985).[UniProtKB:P17763]<ref>PMID:16188985</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Flavivirus langat~~]]	+	[[Category: Langat virus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cowburn, D]]	+	[[Category: Cowburn D]]
-	[[Category: Dutta, K]]	+	[[Category: Dutta K]]
-	[[Category: Fox~~, R O~~]]	+	[[Category: Fox RO]]
-	[[Category: Mukherjee, M]]	+	[[Category: Mukherjee M]]
-	[[Category: White~~, M A]]~~	+	[[Category: White MA]]
-	~~[[Category: Domain iii]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 13:23, 24 November 2021

2021-11-24T13:23:02Z

←Older revision		Revision as of 13:23, 24 November 2021
Line 3:		Line 3:
	<StructureSection load='2gg1' size='340' side='right'caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2gg1' size='340' side='right'caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z66\|1z66]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z66\|1z66]]</div></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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [~~http~~://pdbe.org/2gg1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2gg1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2gg1 ProSAT]</span></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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [https://pdbe.org/2gg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2gg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gg1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/POLG_LANVY POLG_LANVY]] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). 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). 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).	+	[[https://www.uniprot.org/uniprot/POLG_LANVY POLG_LANVY]] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). 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). 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).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:46, 19 February 2020

2020-02-19T06:46:53Z

←Older revision		Revision as of 06:46, 19 February 2020
Line 1:		Line 1:

	==NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)==		==NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)==
-	<StructureSection load='2gg1' size='340' side='right' caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2gg1' size='340' side='right'caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Flavivirus langat]]		[[Category: Flavivirus langat]]
		+	[[Category: Large Structures]]
	[[Category: Cowburn, D]]		[[Category: Cowburn, D]]
	[[Category: Dutta, K]]		[[Category: Dutta, K]]

OCA at 07:15, 20 June 2018

2018-06-20T07:15:29Z

←Older revision		Revision as of 07:15, 20 June 2018
Line 1:		Line 1:
		+
	==NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)==		==NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)==
	<StructureSection load='2gg1' size='340' side='right' caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2gg1' size='340' side='right' caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z66\|1z66]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z66\|1z66]]</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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [http://pdbe.org/2gg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2gg1 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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [http://pdbe.org/2gg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2gg1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gg1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/2gg1_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/2gg1_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=2gg1 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:54, 12 September 2015

2015-09-12T00:54:23Z

←Older revision		Revision as of 00:54, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='2gg1' size='340' side='right' caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2gg1' size='340' side='right' caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Langat_virus Langat virus~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z66\|1z66]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z66\|1z66]]</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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2gg1 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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [http://pdbe.org/2gg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2gg1 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2gg1" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Langat virus~~]]	+	[[Category: Flavivirus langat]]
	[[Category: Cowburn, D]]		[[Category: Cowburn, D]]
	[[Category: Dutta, K]]		[[Category: Dutta, K]]

OCA at 21:40, 25 December 2014

2014-12-25T21:40:22Z

←Older revision		Revision as of 21:40, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z66\|1z66]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z66\|1z66]]</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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2gg1 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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2gg1 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLG_LANVY POLG_LANVY]] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). 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). 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).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Langat virus]]		[[Category: Langat virus]]
-	[[Category: Cowburn, D.]]	+	[[Category: Cowburn, D]]
-	[[Category: Dutta, K.]]	+	[[Category: Dutta, K]]
-	[[Category: Fox, R O.]]	+	[[Category: Fox, R O]]
-	[[Category: Mukherjee, M.]]	+	[[Category: Mukherjee, M]]
-	[[Category: White, M A.]]	+	[[Category: White, M A]]
	[[Category: Domain iii]]		[[Category: Domain iii]]
	[[Category: Viral protein]]		[[Category: Viral protein]]

OCA at 08:55, 30 September 2014

2014-09-30T08:55:12Z

←Older revision		Revision as of 08:55, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2gg1.~~png~~\|~~left~~\|200px]]	+	==NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)==
		+	<StructureSection load='2gg1' size='340' side='right' caption='[[2gg1]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z66\|1z66]]</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=2gg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2gg1 PDBsum]</span></td></tr>
		+	<table>
		+	== 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/gg/2gg1_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Flaviviruses cause many human diseases, including dengue fever, yellow fever, West Nile viral encephalitis, and hemorrhagic fevers, and are transmitted to their vertebrate hosts by infected mosquitoes and ticks. Domain III of the envelope protein (E-D3) is considered to be the primary viral determinant involved in the virus-host-cell receptor interaction, and thus represents an excellent target for antiviral drug development. Langat (LGT) virus is a naturally attenuated BSL-2 TBE virus and is a model for the pathogenic BSL-3 and BSL-4 viruses in the serogroup. We have determined the solution structure of LGT-E-D3 using heteronuclear NMR spectroscopy. The backbone dynamics of LGT-E-D3 have been investigated using 15N relaxation measurements. A detailed analysis of the solution structure and dynamics of LGT-E-D3 suggests potential residues that could form a surface for molecular recognition, and thereby represent a target site for antiviral therapeutics design.

-	~~{{STRUCTURE_2gg1\| PDB=2gg1 \| SCENE= }}~~	+	NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition.,Mukherjee M, Dutta K, White MA, Cowburn D, Fox RO Protein Sci. 2006 Jun;15(6):1342-55. PMID:16731969<ref>PMID:16731969</ref>

-	~~===NMR solution structure of domain III~~ of the ~~E-protein of tick-borne Langat flavivirus (includes RDC restraints)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16731969}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2gg1]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Langat_virus Langat virus]~~. ~~This structure supersedes the now removed PDB entry [http:~~/~~/oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:016731969<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Langat virus]]		[[Category: Langat virus]]
	[[Category: Cowburn, D.]]		[[Category: Cowburn, D.]]

OCA: Protected "2gg1" [edit=sysop:move=sysop]

2013-01-07T13:51:25Z

Protected "2gg1" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:51, 7 January 2013

OCA at 13:51, 7 January 2013

2013-01-07T13:51:22Z

←Older revision		Revision as of 13:51, 7 January 2013
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-	{{Seed}}
	[[Image:2gg1.png\|left\|200px]]		[[Image:2gg1.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2gg1", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2gg1\| PDB=2gg1 \| SCENE= }}		{{STRUCTURE_2gg1\| PDB=2gg1 \| SCENE= }}

	===NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)===		===NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16731969}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16731969 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16731969}}		{{ABSTRACT_PUBMED_16731969}}

	==About this Structure==		==About this Structure==
-	~~2GG1~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA].	+	[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16731969~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016731969</ref><references group="xtra"/>
	[[Category: Langat virus]]		[[Category: Langat virus]]
	[[Category: Cowburn, D.]]		[[Category: Cowburn, D.]]
Line 31:		Line 19:
	[[Category: White, M A.]]		[[Category: White, M A.]]
	[[Category: Domain iii]]		[[Category: Domain iii]]
-	[[Category: Nmr]]
	[[Category: Viral protein]]		[[Category: Viral protein]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:43:26 2009''

OCA at 06:43, 18 February 2009

2009-02-18T06:43:28Z

←Older revision		Revision as of 06:43, 18 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2GG1 is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA].	+	2GG1 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA].

	==Reference==		==Reference==
-	NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition., Mukherjee M, Dutta K, White MA, Cowburn D, Fox RO, Protein Sci. 2006 Jun;15(6):1342-55. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/16731969 16731969]~~	+	<ref group="xtra">PMID:16731969</ref><references group="xtra"/>
	[[Category: Langat virus]]		[[Category: Langat virus]]
-	[[Category: Single protein]]
	[[Category: Cowburn, D.]]		[[Category: Cowburn, D.]]
	[[Category: Dutta, K.]]		[[Category: Dutta, K.]]
Line 35:		Line 34:
	[[Category: Viral protein]]		[[Category: Viral protein]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 14~~:55:~~40 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:43:26 2009''