2rsw - Revision history

OCA at 10:04, 14 June 2023

OCA — Wed, 14 Jun 2023 10:04:04 GMT

←Older revision		Revision as of 10:04, 14 June 2023
Line 1:		Line 1:

	==NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide==		==NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide==
-	<StructureSection load='2rsw' size='340' side='right'caption='[[2rsw~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2rsw' size='340' side='right'caption='[[2rsw]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chikungunya_virus_strain_S27-African_prototype Chikungunya virus strain S27-African prototype]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSW FirstGlance]. <br>
	</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [https://pdbe.org/2rsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [https://www.ebi.ac.uk/pdbsum/2rsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsw ProSAT]</span></td></tr>		</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [https://pdbe.org/2rsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [https://www.ebi.ac.uk/pdbsum/2rsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/POLS_CHIKS POLS_CHIKS]] Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). E3 protein's function is unknown (By similarity). E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane (By similarity). 6K is a constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins (By similarity). E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane (By similarity).	+	[https://www.uniprot.org/uniprot/POLS_CHIKS POLS_CHIKS] Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). E3 protein's function is unknown (By similarity). E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane (By similarity). 6K is a constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins (By similarity). E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Chikungunya virus strain S27-African prototype]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bhattacharjya, S]]	+	[[Category: Bhattacharjya S]]
-	[[Category: Mohanram, H]]	+	[[Category: Mohanram H]]
-	~~[[Category: Dpc]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 12:26, 23 March 2022

OCA — Wed, 23 Mar 2022 12:26:21 GMT

←Older revision		Revision as of 12:26, 23 March 2022
Line 3:		Line 3:
	<StructureSection load='2rsw' size='340' side='right'caption='[[2rsw]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rsw' size='340' side='right'caption='[[2rsw]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2RSW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSW FirstGlance]. <br>
-	</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [~~http~~://pdbe.org/2rsw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2rsw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsw ProSAT]</span></td></tr>	+	</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [https://pdbe.org/2rsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [https://www.ebi.ac.uk/pdbsum/2rsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/POLS_CHIKS POLS_CHIKS]] Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). E3 protein's function is unknown (By similarity). E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane (By similarity). 6K is a constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins (By similarity). E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane (By similarity).	+	[[https://www.uniprot.org/uniprot/POLS_CHIKS POLS_CHIKS]] Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). E3 protein's function is unknown (By similarity). E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane (By similarity). 6K is a constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins (By similarity). E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:05, 17 June 2020

OCA — Wed, 17 Jun 2020 11:05:27 GMT

←Older revision		Revision as of 11:05, 17 June 2020
Line 1:		Line 1:

	==NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide==		==NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide==
-	<StructureSection load='2rsw' size='340' side='right' caption='[[2rsw]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2rsw' size='340' side='right'caption='[[2rsw]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2RSW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RSW FirstGlance]. <br>
-	</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [http://pdbe.org/2rsw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [http://www.ebi.ac.uk/pdbsum/2rsw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsw ProSAT]</span></td></tr>	+	</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [http://pdbe.org/2rsw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [http://www.ebi.ac.uk/pdbsum/2rsw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Bhattacharjya, S]]		[[Category: Bhattacharjya, S]]
	[[Category: Mohanram, H]]		[[Category: Mohanram, H]]
	[[Category: Dpc]]		[[Category: Dpc]]
	[[Category: Viral protein]]		[[Category: Viral protein]]

OCA at 17:15, 4 August 2016

OCA — Thu, 04 Aug 2016 17:15:14 GMT

←Older revision		Revision as of 17:15, 4 August 2016
Line 1:		Line 1:
		+
	==NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide==		==NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide==
	<StructureSection load='2rsw' size='340' side='right' caption='[[2rsw]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rsw' size='340' side='right' caption='[[2rsw]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RSW FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RSW FirstGlance]. <br>
-	</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [http://www.ebi.ac.uk/pdbsum/2rsw PDBsum]</span></td></tr>	+	</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [http://pdbe.org/2rsw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [http://www.ebi.ac.uk/pdbsum/2rsw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	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 2rsw" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:19, 25 December 2014

OCA — Thu, 25 Dec 2014 11:19:02 GMT

←Older revision		Revision as of 11:19, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2rsw\| PDB=2rsw \| SCENE= }}~~	+	==NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide==
-	===NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide===	+	<StructureSection load='2rsw' size='340' side='right' caption='[[2rsw]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_22978677}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RSW FirstGlance]. <br>
-	==Function==	+	</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=2rsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rsw RCSB], [http://www.ebi.ac.uk/pdbsum/2rsw PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/POLS_CHIKS POLS_CHIKS]] Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). E3 protein's function is unknown (By similarity). E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane (By similarity). 6K is a constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins (By similarity). E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane (By similarity).		[[http://www.uniprot.org/uniprot/POLS_CHIKS POLS_CHIKS]] Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). E3 protein's function is unknown (By similarity). E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane (By similarity). 6K is a constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins (By similarity). E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The virus-host cell fusion process is mediated by a membrane anchored viral fusion protein that inserts its hydrophobic fusion peptide into the plasma membrane of the host cell, initiating the fusion reaction. Therefore, fusion peptides are an important functional constituent of the fusion proteins of enveloped viruses. In this work, we characterize the fusion peptide or VT18 (V(84)YPFMWGGAYCFCDAENT(101)) of Chikungunya virus (CHIKV) using NMR and fluorescence spectroscopy in zwitterionic lipid environments. Our results demonstrate that the VT18 peptide is able to induce liposome fusions in a pH independent manner and interacts with the zwitterionic lipid vesicles. The NMR derived three-dimensional structure of VT18, in solution of dodecylphosphocholine (DPC) micelles, is typified by extended or beta-type conformations for most of the residues, whereby residues M88-W89-G90-G91 adopt a type I beta-turn conformation. Strikingly, the aromatic side chains of residues Y85, F87, Y93, and F95 in the VT18 structure are found to be well-packed forming an aromatic core. In particular, residue F87 is situated at the center of the aromatic core establishing a close proximity with other aromatic side chains. Further, the aromatic core residues are also involved in packing interactions with the side chains of residues M88, C94. Paramagnetic relaxation enhancement NMR, using spin labeled doxyl lipids, indicated that the aromatic core residues of VT18 are well inserted into the micelles, whereas the polar residues at the C-terminus may be surface localized. The atomic resolution structure and lipid interactions of CHIKV fusion peptide presented here will aid to uncover the fusion mechanism by the type II viral fusion proteins.

-	~~==About this Structure==~~	+	NMR structure, localization, and vesicle fusion of Chikungunya virus fusion peptide.,Mohanram H, Nip A, Domadia PN, Bhunia A, Bhattacharjya S Biochemistry. 2012 Oct 9;51(40):7863-72. doi: 10.1021/bi300901f. Epub 2012 Sep, 26. PMID:22978677<ref>PMID:22978677</ref>
-	~~[[2rsw]] is a 1 chain~~ structure. ~~Full experimental information is available from [http~~:~~//oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=2RSW OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:022978677</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Bhattacharjya, S.]]	+	== References ==
-	[[Category: Mohanram, H.]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bhattacharjya, S]]
		+	[[Category: Mohanram, H]]
	[[Category: Dpc]]		[[Category: Dpc]]
	[[Category: Viral protein]]		[[Category: Viral protein]]

OCA at 13:55, 19 June 2013

OCA — Wed, 19 Jun 2013 13:55:33 GMT

←Older revision		Revision as of 13:55, 19 June 2013
Line 1:		Line 1:
-	[[Image:2rsw.jpg\|left\|200px]]
-
	{{STRUCTURE_2rsw\| PDB=2rsw \| SCENE= }}		{{STRUCTURE_2rsw\| PDB=2rsw \| SCENE= }}
-
	===NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide===		===NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide===
		+	{{ABSTRACT_PUBMED_22978677}}

		+	==Function==
		+	[[http://www.uniprot.org/uniprot/POLS_CHIKS POLS_CHIKS]] Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). E3 protein's function is unknown (By similarity). E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane (By similarity). 6K is a constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins (By similarity). E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane (By similarity).

	==About this Structure==		==About this Structure==
	[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA].		[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022978677</ref><references group="xtra"/><references/>
	[[Category: Bhattacharjya, S.]]		[[Category: Bhattacharjya, S.]]
	[[Category: Mohanram, H.]]		[[Category: Mohanram, H.]]
	[[Category: Dpc]]		[[Category: Dpc]]
	[[Category: Viral protein]]		[[Category: Viral protein]]

OCA at 05:17, 12 September 2012

OCA — Wed, 12 Sep 2012 05:17:46 GMT

←Older revision		Revision as of 05:17, 12 September 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:2rsw.jpg\|left\|200px]]

-	~~The entry~~ 2rsw ~~is ON HOLD~~	+	{{STRUCTURE_2rsw\| PDB=2rsw \| SCENE= }}

-	~~Authors: Mohanram~~, ~~H., Bhattacharjya, S.~~	+	===NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide===

-	~~Description: NMR~~ structure, ~~Localization and Vesicle fusion of Chikungunya virus Fusion peptide~~	+
		+	==About this Structure==
		+	[[2rsw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSW OCA].
		+	[[Category: Bhattacharjya, S.]]
		+	[[Category: Mohanram, H.]]
		+	[[Category: Dpc]]
		+	[[Category: Viral protein]]

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

OCA — Wed, 01 Aug 2012 05:10:23 GMT

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

←Older revision

Revision as of 05:10, 1 August 2012

OCA: New page: '''Unreleased structure''' The entry 2rsw is ON HOLD Authors: Mohanram, H., Bhattacharjya, S. Description: NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion pe...

OCA — Wed, 01 Aug 2012 05:10:23 GMT

New page: '''Unreleased structure''' The entry 2rsw is ON HOLD Authors: Mohanram, H., Bhattacharjya, S. Description: NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion pe...

New page

'''Unreleased structure'''

The entry 2rsw is ON HOLD

Authors: Mohanram, H., Bhattacharjya, S.

Description: NMR structure, Localization and Vesicle fusion of Chikungunya virus Fusion peptide