3c6d - Revision history

OCA at 09:33, 21 February 2024

2024-02-21T09:33:16Z

←Older revision		Revision as of 09:33, 21 February 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/A7TUD3_9FLAV A7TUD3_9FLAV] Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.[ARBA:ARBA00024317] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504] Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859]		[https://www.uniprot.org/uniprot/A7TUD3_9FLAV A7TUD3_9FLAV] Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.[ARBA:ARBA00024317] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504] Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Many viruses go through a maturation step in the final stages of assembly before being transmitted to another host. The maturation process of flaviviruses is directed by the proteolytic cleavage of the precursor membrane protein (prM), turning inert virus into infectious particles. We have determined the 2.2 angstrom resolution crystal structure of a recombinant protein in which the dengue virus prM is linked to the envelope glycoprotein E. The structure represents the prM-E heterodimer and fits well into the cryo-electron microscopy density of immature virus at neutral pH. The pr peptide beta-barrel structure covers the fusion loop in E, preventing fusion with host cell membranes. The structure provides a basis for identifying the stages of its pH-directed conformational metamorphosis during maturation, ending with release of pr when budding from the host.
-
-	The flavivirus precursor membrane-envelope protein complex: structure and maturation.,Li L, Lok SM, Yu IM, Zhang Y, Kuhn RJ, Chen J, Rossmann MG Science. 2008 Mar 28;319(5871):1830-4. PMID:18369147<ref>PMID:18369147</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3c6d" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</SX>		</SX>

OCA at 18:09, 1 November 2023

2023-11-01T18:09:58Z

←Older revision		Revision as of 18:09, 1 November 2023
Line 3:		Line 3:
	<SX load='3c6d' size='340' side='right' viewer='molstar' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>		<SX load='3c6d' size='340' side='right' viewer='molstar' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [https://en.wikipedia.org/wiki/~~Dengue_virus_2_thailand~~/16681/84 Dengue virus 2 ~~thailand~~/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C6D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [https://en.wikipedia.org/wiki/Dengue_virus_2_Thailand/16681/84 Dengue virus 2 Thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C6D 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;'~~>[[~~3c5x~~\|~~3c5x~~]]~~</div>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 12.5Å</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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [https://pdbe.org/3c6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [https://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d 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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [https://pdbe.org/3c6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [https://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~O11875_9FLAV O11875_9FLAV~~]] 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).[SAAS:SAAS026470_004_099774] [[https://www.uniprot.org/uniprot/POLG_DEN28 POLG_DEN28]] 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). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome (By similarity). Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential). Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity). 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). 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). Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter ~~(By similarity)~~. ~~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)~~. ~~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 TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).	+	[https://www.uniprot.org/uniprot/A7TUD3_9FLAV A7TUD3_9FLAV] Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.[ARBA:ARBA00024317] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504] Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	</SX>		</SX>
	[[Category: Dengue virus 2]]		[[Category: Dengue virus 2]]
-	[[Category: Dengue virus 2 ~~thailand~~/16681/84]]	+	[[Category: Dengue virus 2 Thailand/16681/84]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Li, L]]	+	[[Category: Li L]]
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: Capsid protein]]~~	+
-	~~[[Category: Cleavage on pair of basic residue]]~~	+
-	~~[[Category: Endoplasmic reticulum]]~~	+
-	~~[[Category: Envelope protein]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Helicase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Icosahedral virion]]~~	+
-	~~[[Category: Icosahedral virus]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Multifunctional enzyme]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Nucleotidyltransferase]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Ribonucleoprotein]]~~	+
-	~~[[Category: Rna replication]]~~	+
-	~~[[Category: Rna-binding]]~~	+
-	~~[[Category: Rna-directed rna polymerase]]~~	+
-	~~[[Category: Secreted]]~~	+
-	~~[[Category: Serine protease]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Transcription regulation]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transmembrane]]~~	+
-	~~[[Category: Viral nucleoprotein]]~~	+
-	~~[[Category: Virus~~]]	+

OCA at 07:45, 27 January 2022

2022-01-27T07:45:06Z

←Older revision		Revision as of 07:45, 27 January 2022
Line 3:		Line 3:
	<SX load='3c6d' size='340' side='right' viewer='molstar' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>		<SX load='3c6d' size='340' side='right' viewer='molstar' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [~~http~~://en.wikipedia.org/wiki/Dengue_virus_2_thailand/16681/84 Dengue virus 2 thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3C6D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [https://en.wikipedia.org/wiki/Dengue_virus_2_thailand/16681/84 Dengue virus 2 thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C6D FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c5x\|3c5x]]</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;'>[[3c5x\|3c5x]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [~~http~~://pdbe.org/3c6d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d 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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [https://pdbe.org/3c6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [https://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/O11875_9FLAV O11875_9FLAV]] 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).[SAAS:SAAS026470_004_099774] [[~~http~~://www.uniprot.org/uniprot/POLG_DEN28 POLG_DEN28]] 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). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome (By similarity). Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential). Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity). 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). 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). Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter (By similarity). 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). 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 TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).	+	[[https://www.uniprot.org/uniprot/O11875_9FLAV O11875_9FLAV]] 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).[SAAS:SAAS026470_004_099774] [[https://www.uniprot.org/uniprot/POLG_DEN28 POLG_DEN28]] 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). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome (By similarity). Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential). Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity). 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). 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). Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter (By similarity). 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). 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 TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:14, 10 April 2020

2020-04-10T17:14:01Z

←Older revision		Revision as of 17:14, 10 April 2020
Line 3:		Line 3:
	<SX load='3c6d' size='340' side='right' viewer='molstar' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>		<SX load='3c6d' size='340' side='right' viewer='molstar' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [http://en.wikipedia.org/wiki/Dengue_virus_2_thailand/16681/84 Dengue virus 2 thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3C6D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [http://en.wikipedia.org/wiki/Dengue_virus_2_thailand/16681/84 Dengue virus 2 thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3C6D FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c5x\|3c5x]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c5x\|3c5x]]</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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://pdbe.org/3c6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://pdbe.org/3c6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:05, 6 March 2020

2020-03-06T17:05:04Z

←Older revision		Revision as of 17:05, 6 March 2020
Line 1:		Line 1:

	==The pseudo-atomic structure of dengue immature virus==		==The pseudo-atomic structure of dengue immature virus==
-	<~~StructureSection~~ load='3c6d' size='340' side='right' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>	+	<SX load='3c6d' size='340' side='right' viewer='molstar' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [http://en.wikipedia.org/wiki/Dengue_virus_2_thailand/16681/84 Dengue virus 2 thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C6D FirstGlance]. <br>		<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [http://en.wikipedia.org/wiki/Dengue_virus_2_thailand/16681/84 Dengue virus 2 thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C6D FirstGlance]. <br>
Line 21:		Line 21:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Dengue virus 2]]		[[Category: Dengue virus 2]]
	[[Category: Dengue virus 2 thailand/16681/84]]		[[Category: Dengue virus 2 thailand/16681/84]]
		+	[[Category: Large Structures]]
	[[Category: Li, L]]		[[Category: Li, L]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]

OCA at 07:54, 18 July 2018

2018-07-18T07:54:40Z

←Older revision		Revision as of 07:54, 18 July 2018
Line 3:		Line 3:
	<StructureSection load='3c6d' size='340' side='right' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>		<StructureSection load='3c6d' size='340' side='right' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Den26 Den26~~] and [http://en.wikipedia.org/wiki/~~Dengue_virus_2~~ Dengue virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C6D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [http://en.wikipedia.org/wiki/Dengue_virus_2_thailand/16681/84 Dengue virus 2 thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C6D FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c5x\|3c5x]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c5x\|3c5x]]</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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://pdbe.org/3c6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d ProSAT]</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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://pdbe.org/3c6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d ProSAT]</span></td></tr>
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Den26]]
	[[Category: Dengue virus 2]]		[[Category: Dengue virus 2]]
		+	[[Category: Dengue virus 2 thailand/16681/84]]
	[[Category: Li, L]]		[[Category: Li, L]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]

OCA at 23:54, 4 August 2016

2016-08-04T23:54:41Z

←Older revision		Revision as of 23:54, 4 August 2016
Line 1:		Line 1:
		+
	==The pseudo-atomic structure of dengue immature virus==		==The pseudo-atomic structure of dengue immature virus==
	<StructureSection load='3c6d' size='340' side='right' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>		<StructureSection load='3c6d' size='340' side='right' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Dengue_virus_2 Dengue virus 2~~] and [http://en.wikipedia.org/wiki/~~Dengue_virus_2_thailand/16681/84~~ Dengue virus 2 ~~thailand/16681/84~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C6D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Den26 Den26] and [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C6D FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c5x\|3c5x]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c5x\|3c5x]]</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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d 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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://pdbe.org/3c6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/POLG_DEN28 POLG_DEN28]] 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). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome (By similarity). Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential). Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity). 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). 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). Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter (By similarity). 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). 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 TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).	+	[[http://www.uniprot.org/uniprot/O11875_9FLAV O11875_9FLAV]] 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).[SAAS:SAAS026470_004_099774] [[http://www.uniprot.org/uniprot/POLG_DEN28 POLG_DEN28]] 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). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome (By similarity). Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential). Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity). 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). 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). Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter (By similarity). 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). 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 TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 16:		Line 17:
	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 3c6d" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Den26]]
	[[Category: Dengue virus 2]]		[[Category: Dengue virus 2]]
-	[[Category: Dengue virus 2 thailand/16681/84]]
	[[Category: Li, L]]		[[Category: Li, L]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]

OCA at 20:55, 24 December 2014

2014-12-24T20:55:29Z

←Older revision		Revision as of 20:55, 24 December 2014
Line 6:		Line 6:
	<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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d 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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLG_DEN28 POLG_DEN28]] 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). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome (By similarity). Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential). Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity). 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). 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). Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter (By similarity). 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). 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 TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 22:
	[[Category: Dengue virus 2]]		[[Category: Dengue virus 2]]
	[[Category: Dengue virus 2 thailand/16681/84]]		[[Category: Dengue virus 2 thailand/16681/84]]
-	[[Category: Li, L.]]	+	[[Category: Li, L]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Capsid protein]]		[[Category: Capsid protein]]

OCA at 09:19, 5 November 2014

2014-11-05T09:19:19Z

←Older revision		Revision as of 09:19, 5 November 2014
Line 1:		Line 1:
-	[[~~Image:~~3c6d.~~png~~\|~~left~~\|~~200px~~]]	+	==The pseudo-atomic structure of dengue immature virus==
		+	<StructureSection load='3c6d' size='340' side='right' caption='[[3c6d]], [[Resolution\|resolution]] 12.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3c6d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [http://en.wikipedia.org/wiki/Dengue_virus_2_thailand/16681/84 Dengue virus 2 thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C6D FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c5x\|3c5x]]</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=3c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c6d RCSB], [http://www.ebi.ac.uk/pdbsum/3c6d PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Many viruses go through a maturation step in the final stages of assembly before being transmitted to another host. The maturation process of flaviviruses is directed by the proteolytic cleavage of the precursor membrane protein (prM), turning inert virus into infectious particles. We have determined the 2.2 angstrom resolution crystal structure of a recombinant protein in which the dengue virus prM is linked to the envelope glycoprotein E. The structure represents the prM-E heterodimer and fits well into the cryo-electron microscopy density of immature virus at neutral pH. The pr peptide beta-barrel structure covers the fusion loop in E, preventing fusion with host cell membranes. The structure provides a basis for identifying the stages of its pH-directed conformational metamorphosis during maturation, ending with release of pr when budding from the host.

-	~~{{STRUCTURE_3c6d\| PDB=3c6d \| SCENE= }}~~	+	The flavivirus precursor membrane-envelope protein complex: structure and maturation.,Li L, Lok SM, Yu IM, Zhang Y, Kuhn RJ, Chen J, Rossmann MG Science. 2008 Mar 28;319(5871):1830-4. PMID:18369147<ref>PMID:18369147</ref>

-	~~===The pseudo-atomic structure~~ of ~~dengue immature virus===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18369147}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[3c6d]] is a 6 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Dengue_virus_2 Dengue virus 2] and [http://en~~.~~wikipedia.org~~/~~wiki/Viruses Viruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6D OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:018369147<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Dengue virus 2]]		[[Category: Dengue virus 2]]
-	[[Category: ~~Viruses~~]]	+	[[Category: Dengue virus 2 thailand/16681/84]]
	[[Category: Li, L.]]		[[Category: Li, L.]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]

OCA: Protected "3c6d" [edit=sysop:move=sysop]

2013-01-07T21:51:56Z

Protected "3c6d" [edit=sysop:move=sysop]

←Older revision

Revision as of 21:51, 7 January 2013