1p5w - Revision history

OCA at 06:10, 3 April 2024

OCA — Wed, 03 Apr 2024 06:10:13 GMT

←Older revision		Revision as of 06:10, 3 April 2024
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	<StructureSection load='1p5w' size='340' side='right'caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='1p5w' size='340' side='right'caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Cpv Cpv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P5W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P5W FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.3Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;~~'>~~[[1p5y\|1p5y]]~~</~~div~~></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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [https://pdbe.org/1p5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [https://www.ebi.ac.uk/pdbsum/1p5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5w 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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [https://pdbe.org/1p5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [https://www.ebi.ac.uk/pdbsum/1p5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CAPSD_PAVCD CAPSD_PAVCD]] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptor TFRC. This attachment induces virion internalization predominantly through clathrin-endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>	+	[https://www.uniprot.org/uniprot/CAPSD_PAVCD CAPSD_PAVCD] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptor TFRC. This attachment induces virion internalization predominantly through clathrin-endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1p5w 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=1p5w ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Canine parvovirus (CPV) and feline panleukopenia virus (FPV) differ in their ability to infect dogs and dog cells. Canine cell infection is a specific property of CPV and depends on the ability of the virus to bind the canine transferrin receptor (TfR), as well as other unidentified factors. Three regions in the capsid structure, located around VP2 residues 93, 300, and 323, can all influence canine TfR binding and canine cell infection. These regions were compared in the CPV and FPV capsid structures that have been determined, as well as in two new structures of CPV capsids that contain substitutions of the VP2 Asn-93 to Asp and Arg, respectively. The new structures, determined by X-ray crystallography to 3.2 and 3.3 A resolutions, respectively, clearly showed differences in the interactions of residue 93 with an adjacent loop on the capsid surface. Each of the three regions show small differences in structure, but each appears to be structurally independent of the others, and the changes likely act together to affect the ability of the capsid to bind the canine TfR and to infect canine cells. This emphasizes the complex nature of capsid alterations that change the virus-cell interaction to allow infection of cells from different hosts.
-
-	Structures of host range-controlling regions of the capsids of canine and feline parvoviruses and mutants.,Govindasamy L, Hueffer K, Parrish CR, Agbandje-McKenna M J Virol. 2003 Nov;77(22):12211-21. PMID:14581558<ref>PMID:14581558</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1p5w" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cpv~~]]	+	[[Category: Canine parvovirus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Agbandje-McKenna, M]]	+	[[Category: Agbandje-McKenna M]]
-	[[Category: Govindasamy, L]]	+	[[Category: Govindasamy L]]
-	~~[[Category: Canine parvovirus]]~~	+
-	~~[[Category: Icosahedral virus]]~~	+
-	~~[[Category: Parvovirade]]~~	+
-	~~[[Category: Virus-dna complex~~]]	+

OCA at 09:25, 8 September 2021

OCA — Wed, 08 Sep 2021 09:25:36 GMT

←Older revision		Revision as of 09:25, 8 September 2021
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	<StructureSection load='1p5w' size='340' side='right'caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='1p5w' size='340' side='right'caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Cpv Cpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1P5W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cpv Cpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P5W FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p5y\|1p5y]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p5y\|1p5y]]</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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [~~http~~://pdbe.org/1p5w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1p5w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5w 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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [https://pdbe.org/1p5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [https://www.ebi.ac.uk/pdbsum/1p5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CAPSD_PAVCD CAPSD_PAVCD]] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptor TFRC. This attachment induces virion internalization predominantly through clathrin-endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>	+	[[https://www.uniprot.org/uniprot/CAPSD_PAVCD CAPSD_PAVCD]] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptor TFRC. This attachment induces virion internalization predominantly through clathrin-endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Canine parvovirus\|Canine parvovirus]]		*[[Canine parvovirus\|Canine parvovirus]]
-	*[[Virus coat ~~protein~~\|Virus coat ~~protein~~]]	+	*[[Virus coat proteins 3D structures\|Virus coat proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:26, 27 November 2019

OCA — Wed, 27 Nov 2019 10:26:42 GMT

←Older revision		Revision as of 10:26, 27 November 2019
Line 1:		Line 1:

	==The structures of host range controlling regions of the capsids of canine and feline parvoviruses and mutants==		==The structures of host range controlling regions of the capsids of canine and feline parvoviruses and mutants==
-	<StructureSection load='1p5w' size='340' side='right' caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>	+	<StructureSection load='1p5w' size='340' side='right'caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cpv Cpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P5W FirstGlance]. <br>		<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cpv Cpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P5W FirstGlance]. <br>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1p5w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1p5w" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Canine parvovirus\|Canine parvovirus]]
		+	*[[Virus coat protein\|Virus coat protein]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Cpv]]		[[Category: Cpv]]
		+	[[Category: Large Structures]]
	[[Category: Agbandje-McKenna, M]]		[[Category: Agbandje-McKenna, M]]
	[[Category: Govindasamy, L]]		[[Category: Govindasamy, L]]

OCA at 07:54, 15 February 2018

OCA — Thu, 15 Feb 2018 07:54:53 GMT

←Older revision		Revision as of 07:54, 15 February 2018
Line 1:		Line 1:
		+
	==The structures of host range controlling regions of the capsids of canine and feline parvoviruses and mutants==		==The structures of host range controlling regions of the capsids of canine and feline parvoviruses and mutants==
	<StructureSection load='1p5w' size='340' side='right' caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='1p5w' size='340' side='right' caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p5y\|1p5y]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p5y\|1p5y]]</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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [http://pdbe.org/1p5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [http://www.ebi.ac.uk/pdbsum/1p5w 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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [http://pdbe.org/1p5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [http://www.ebi.ac.uk/pdbsum/1p5w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p5w_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p5w_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>
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1p5w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1p5w" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Virus coat protein\|Virus coat protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:05, 8 February 2016

OCA — Mon, 08 Feb 2016 12:05:45 GMT

←Older revision		Revision as of 12:05, 8 February 2016
Line 18:		Line 18:
	<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=1p5w ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 11:24, 10 September 2015

OCA — Thu, 10 Sep 2015 11:24:33 GMT

←Older revision		Revision as of 11:24, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1p5w' size='340' side='right' caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='1p5w' size='340' side='right' caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Canine_parvovirus Canine parvovirus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P5W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cpv Cpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P5W FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p5y\|1p5y]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p5y\|1p5y]]</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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [http://www.ebi.ac.uk/pdbsum/1p5w 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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [http://pdbe.org/1p5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [http://www.ebi.ac.uk/pdbsum/1p5w PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~COAT_PAVCD COAT_PAVCD~~]] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptor TFRC. This attachment induces virion internalization predominantly through clathrin-endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>	+	[[http://www.uniprot.org/uniprot/CAPSD_PAVCD CAPSD_PAVCD]] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptor TFRC. This attachment induces virion internalization predominantly through clathrin-endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 28:		Line 28:
	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 1p5w" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Canine parvovirus~~]]	+	[[Category: Cpv]]
	[[Category: Agbandje-McKenna, M]]		[[Category: Agbandje-McKenna, M]]
	[[Category: Govindasamy, L]]		[[Category: Govindasamy, L]]
		+	[[Category: Canine parvovirus]]
	[[Category: Icosahedral virus]]		[[Category: Icosahedral virus]]
	[[Category: Parvovirade]]		[[Category: Parvovirade]]
	[[Category: Virus-dna complex]]		[[Category: Virus-dna complex]]

OCA at 23:11, 24 December 2014

OCA — Wed, 24 Dec 2014 23:11:18 GMT

←Older revision		Revision as of 23:11, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P5W FirstGlance]. <br>		<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P5W FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p5y\|1p5y]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p5y\|1p5y]]</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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [http://www.ebi.ac.uk/pdbsum/1p5w 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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [http://www.ebi.ac.uk/pdbsum/1p5w PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/COAT_PAVCD COAT_PAVCD]] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptor TFRC. This attachment induces virion internalization predominantly through clathrin-endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Canine parvovirus]]		[[Category: Canine parvovirus]]
-	[[Category: Agbandje-McKenna, M.]]	+	[[Category: Agbandje-McKenna, M]]
-	[[Category: Govindasamy, L~~.]]~~	+	[[Category: Govindasamy, L]]
-	~~[[Category: Canine parvovirus~~]]	+
	[[Category: Icosahedral virus]]		[[Category: Icosahedral virus]]
	[[Category: Parvovirade]]		[[Category: Parvovirade]]
	[[Category: Virus-dna complex]]		[[Category: Virus-dna complex]]

OCA at 20:36, 28 September 2014

OCA — Sun, 28 Sep 2014 20:36:03 GMT

←Older revision		Revision as of 20:36, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1p5w.~~png~~\|~~left~~\|200px]]	+	==The structures of host range controlling regions of the capsids of canine and feline parvoviruses and mutants==
		+	<StructureSection load='1p5w' size='340' side='right' caption='[[1p5w]], [[Resolution\|resolution]] 3.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1p5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P5W FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1p5y\|1p5y]]</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=1p5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p5w RCSB], [http://www.ebi.ac.uk/pdbsum/1p5w 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/p5/1p5w_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 ==
		+	Canine parvovirus (CPV) and feline panleukopenia virus (FPV) differ in their ability to infect dogs and dog cells. Canine cell infection is a specific property of CPV and depends on the ability of the virus to bind the canine transferrin receptor (TfR), as well as other unidentified factors. Three regions in the capsid structure, located around VP2 residues 93, 300, and 323, can all influence canine TfR binding and canine cell infection. These regions were compared in the CPV and FPV capsid structures that have been determined, as well as in two new structures of CPV capsids that contain substitutions of the VP2 Asn-93 to Asp and Arg, respectively. The new structures, determined by X-ray crystallography to 3.2 and 3.3 A resolutions, respectively, clearly showed differences in the interactions of residue 93 with an adjacent loop on the capsid surface. Each of the three regions show small differences in structure, but each appears to be structurally independent of the others, and the changes likely act together to affect the ability of the capsid to bind the canine TfR and to infect canine cells. This emphasizes the complex nature of capsid alterations that change the virus-cell interaction to allow infection of cells from different hosts.

-	~~{{STRUCTURE_1p5w\| PDB=1p5w \| SCENE= }}~~	+	Structures of host range-controlling regions of the capsids of canine and feline parvoviruses and mutants.,Govindasamy L, Hueffer K, Parrish CR, Agbandje-McKenna M J Virol. 2003 Nov;77(22):12211-21. PMID:14581558<ref>PMID:14581558</ref>

-	~~===The structures of host range controlling regions~~ of the ~~capsids of canine and feline parvoviruses and mutants===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14581558}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1p5w]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Canine_parvovirus Canine parvovirus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA].~~	+

	==See Also==		==See Also==
	*[[Virus coat protein\|Virus coat protein]]		*[[Virus coat protein\|Virus coat protein]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:014581558<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Canine parvovirus]]		[[Category: Canine parvovirus]]
	[[Category: Agbandje-McKenna, M.]]		[[Category: Agbandje-McKenna, M.]]

OCA: Protected "1p5w" [edit=sysop:move=sysop]

OCA — Sat, 20 Oct 2012 10:04:39 GMT

Protected "1p5w" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:04, 20 October 2012

OCA at 10:04, 20 October 2012

OCA — Sat, 20 Oct 2012 10:04:37 GMT

←Older revision		Revision as of 10:04, 20 October 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1p5w.png\|left\|200px]]		[[Image:1p5w.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1p5w", 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_1p5w\| PDB=1p5w \| SCENE= }}		{{STRUCTURE_1p5w\| PDB=1p5w \| SCENE= }}

	===The structures of host range controlling regions of the capsids of canine and feline parvoviruses and mutants===		===The structures of host range controlling regions of the capsids of canine and feline parvoviruses and mutants===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_14581558}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 14581558 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_14581558}}		{{ABSTRACT_PUBMED_14581558}}

	==About this Structure==		==About this Structure==
-	~~1P5W~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA].	+	[[1p5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5W OCA].
		+
		+	==See Also==
		+	*[[Virus coat protein\|Virus coat protein]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~14581558~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:014581558</ref><references group="xtra"/>
	[[Category: Canine parvovirus]]		[[Category: Canine parvovirus]]
	[[Category: Agbandje-McKenna, M.]]		[[Category: Agbandje-McKenna, M.]]
Line 30:		Line 21:
	[[Category: Icosahedral virus]]		[[Category: Icosahedral virus]]
	[[Category: Parvovirade]]		[[Category: Parvovirade]]
-		+	[[Category: Virus-dna complex]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Feb 16 21:52:05 2009''~~	+