1ruj - Revision history

OCA at 09:06, 22 May 2024

2024-05-22T09:06:34Z

←Older revision		Revision as of 09:06, 22 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhinovirus_B14 Rhinovirus B14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhinovirus_B14 Rhinovirus B14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RUJ 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [https://pdbe.org/1ruj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [https://www.ebi.ac.uk/pdbsum/1ruj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ruj ProSAT]</span></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]] 3Å</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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [https://pdbe.org/1ruj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [https://www.ebi.ac.uk/pdbsum/1ruj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ruj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 07:38, 18 January 2023

2023-01-18T07:38:30Z

←Older revision		Revision as of 07:38, 18 January 2023
Line 3:		Line 3:
	<StructureSection load='1ruj' size='340' side='right'caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1ruj' size='340' side='right'caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Hrv-14 Hrv-14~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhinovirus_B14 Rhinovirus B14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RUJ 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [https://pdbe.org/1ruj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [https://www.ebi.ac.uk/pdbsum/1ruj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ruj 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [https://pdbe.org/1ruj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [https://www.ebi.ac.uk/pdbsum/1ruj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ruj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/POLG_HRV14 POLG_HRV14]] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with human ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. VP0 precursor is a component of immature procapsids (By similarity). Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity). Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity). Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity). Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).	+	[https://www.uniprot.org/uniprot/POLG_HRV14 POLG_HRV14] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with human ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. VP0 precursor is a component of immature procapsids (By similarity). Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity). Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity). Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity). Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Hrv-14]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hadfield, A]]	+	[[Category: Rhinovirus B14]]
-	[[Category: Heinz~~, B A~~]]	+	[[Category: Hadfield A]]
-	[[Category: Kim~~, K H~~]]	+	[[Category: Heinz BA]]
-	[[Category: Kremer~~, M J~~]]	+	[[Category: Kim KH]]
-	[[Category: Minor, I]]	+	[[Category: Kremer MJ]]
-	[[Category: Oliveira~~, M A~~]]	+	[[Category: Minor I]]
-	[[Category: Pevear~~, D C~~]]	+	[[Category: Oliveira MA]]
-	[[Category: Rossmann~~, M G~~]]	+	[[Category: Pevear DC]]
-	[[Category: Rueckert~~, R R~~]]	+	[[Category: Rossmann MG]]
-	[[Category: Shepard, D]]	+	[[Category: Rueckert RR]]
-	~~[[Category: Icosahedral virus]]~~	+	[[Category: Shepard D]]
-	~~[[Category: Rhinovirus coat protein]]~~	+
-	~~[[Category: Virus~~]]	+

OCA at 07:22, 22 September 2021

2021-09-22T07:22:06Z

←Older revision		Revision as of 07:22, 22 September 2021
Line 3:		Line 3:
	<StructureSection load='1ruj' size='340' side='right'caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1ruj' size='340' side='right'caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Hrv-14 Hrv-14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hrv-14 Hrv-14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RUJ 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [~~http~~://pdbe.org/1ruj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ruj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ruj 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [https://pdbe.org/1ruj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [https://www.ebi.ac.uk/pdbsum/1ruj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ruj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/POLG_HRV14 POLG_HRV14]] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with human ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. VP0 precursor is a component of immature procapsids (By similarity). Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity). Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity). Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity). Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).	+	[[https://www.uniprot.org/uniprot/POLG_HRV14 POLG_HRV14]] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with human ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. VP0 precursor is a component of immature procapsids (By similarity). Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity). Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity). Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity). Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 19:03, 11 December 2019

2019-12-11T19:03:01Z

←Older revision		Revision as of 19:03, 11 December 2019
Line 1:		Line 1:

	==RHINOVIRUS 14 MUTANT WITH SER 1 223 REPLACED BY GLY (S1223G)==		==RHINOVIRUS 14 MUTANT WITH SER 1 223 REPLACED BY GLY (S1223G)==
-	<StructureSection load='1ruj' size='340' side='right' caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='1ruj' size='340' side='right'caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrv-14 Hrv-14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrv-14 Hrv-14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Hrv-14]]		[[Category: Hrv-14]]
		+	[[Category: Large Structures]]
	[[Category: Hadfield, A]]		[[Category: Hadfield, A]]
	[[Category: Heinz, B A]]		[[Category: Heinz, B A]]

OCA at 06:34, 8 March 2018

2018-03-08T06:34:46Z

←Older revision		Revision as of 06:34, 8 March 2018
Line 1:		Line 1:
		+
	==RHINOVIRUS 14 MUTANT WITH SER 1 223 REPLACED BY GLY (S1223G)==		==RHINOVIRUS 14 MUTANT WITH SER 1 223 REPLACED BY GLY (S1223G)==
	<StructureSection load='1ruj' size='340' side='right' caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1ruj' size='340' side='right' caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrv-14 Hrv-14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrv-14 Hrv-14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [http://pdbe.org/1ruj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [http://www.ebi.ac.uk/pdbsum/1ruj 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [http://pdbe.org/1ruj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [http://www.ebi.ac.uk/pdbsum/1ruj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ruj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 11:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ru/1ruj_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ru/1ruj_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ruj ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:24, 11 September 2015

2015-09-11T07:24:45Z

←Older revision		Revision as of 07:24, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1ruj' size='340' side='right' caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1ruj' size='340' side='right' caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human_rhinovirus_b14 Human rhinovirus b14~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrv-14 Hrv-14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [http://www.ebi.ac.uk/pdbsum/1ruj 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [http://pdbe.org/1ruj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [http://www.ebi.ac.uk/pdbsum/1ruj PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 25:		Line 25:
	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 1ruj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human rhinovirus b14~~]]	+	[[Category: Hrv-14]]
	[[Category: Hadfield, A]]		[[Category: Hadfield, A]]
	[[Category: Heinz, B A]]		[[Category: Heinz, B A]]

OCA at 13:11, 25 December 2014

2014-12-25T13:11:17Z

←Older revision		Revision as of 13:11, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_b14 Human rhinovirus b14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_b14 Human rhinovirus b14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>
-	</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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [http://www.ebi.ac.uk/pdbsum/1ruj 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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [http://www.ebi.ac.uk/pdbsum/1ruj PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLG_HRV14 POLG_HRV14]] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with human ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. VP0 precursor is a component of immature procapsids (By similarity). Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity). Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity). Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity). Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Human rhinovirus b14]]		[[Category: Human rhinovirus b14]]
-	[[Category: Hadfield, A.]]	+	[[Category: Hadfield, A]]
-	[[Category: Heinz, B A.]]	+	[[Category: Heinz, B A]]
-	[[Category: Kim, K H.]]	+	[[Category: Kim, K H]]
-	[[Category: Kremer, M J.]]	+	[[Category: Kremer, M J]]
-	[[Category: Minor, I.]]	+	[[Category: Minor, I]]
-	[[Category: Oliveira, M A.]]	+	[[Category: Oliveira, M A]]
-	[[Category: Pevear, D C.]]	+	[[Category: Pevear, D C]]
-	[[Category: Rossmann, M G.]]	+	[[Category: Rossmann, M G]]
-	[[Category: Rueckert, R R.]]	+	[[Category: Rueckert, R R]]
-	[[Category: Shepard, D.]]	+	[[Category: Shepard, D]]
	[[Category: Icosahedral virus]]		[[Category: Icosahedral virus]]
	[[Category: Rhinovirus coat protein]]		[[Category: Rhinovirus coat protein]]
	[[Category: Virus]]		[[Category: Virus]]

OCA at 10:10, 3 October 2014

2014-10-03T10:10:45Z

←Older revision		Revision as of 10:10, 3 October 2014
Line 1:		Line 1:
-	[[~~Image~~:1ruj.~~png\|left~~\|200px]]	+	==RHINOVIRUS 14 MUTANT WITH SER 1 223 REPLACED BY GLY (S1223G)==
		+	<StructureSection load='1ruj' size='340' side='right' caption='[[1ruj]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_b14 Human rhinovirus b14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RUJ FirstGlance]. <br>
		+	</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=1ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ruj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ruj RCSB], [http://www.ebi.ac.uk/pdbsum/1ruj 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/ru/1ruj_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 ==
		+	Structures have been determined of three human rhinovirus 14 (HRV14) compensation mutants that have resistance to the antiviral capsid binding compounds WIN 52035 and WIN 52084. In addition, the structure of HRV14 is reported, with a site-directed mutation at residue 1219 in VP1. A spontaneous mutation occurs at the same site in one of the compensation mutants. Some of the mutations are on the viral surface in the canyon and some lie within the hydrophobic binding pocket in VP1 below the ICAM footprint. Those mutant virus strains with mutations on the surface bind better to cells than does wild-type virus. The antiviral compounds bind to the mutant viruses in a manner similar to their binding to wild-type virus. The receptor and WIN compound binding sites overlap, causing competition between receptor attachment and antiviral compound binding. The compensation mutants probably function by shifting the equilibrium in favor of receptor binding. The mutations in the canyon increase the affinity of the virus for the receptor, while the mutations in the pocket probably decrease the affinity of the WIN compounds for the virus by reducing favorable hydrophobic contacts and constricting the pore through which the antiviral compounds are thought to enter the pocket. This is in contrast to the resistant exclusion mutants that block compounds from binding by increasing the bulk of residues within the hydrophobic pocket in VP1.

-	~~{{STRUCTURE_1ruj\| PDB=1ruj \| SCENE= }}~~	+	Structural studies on human rhinovirus 14 drug-resistant compensation mutants.,Hadfield AT, Oliveira MA, Kim KH, Minor I, Kremer MJ, Heinz BA, Shepard D, Pevear DC, Rueckert RR, Rossmann MG J Mol Biol. 1995 Oct 13;253(1):61-73. PMID:7473717<ref>PMID:7473717</ref>

-	~~===RHINOVIRUS 14 MUTANT WITH SER 1 223 REPLACED BY GLY (S1223G)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_7473717}}~~	+	==See Also==
-		+	*[[Human rhinovirus\|Human rhinovirus]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_b14~~ Human rhinovirus ~~b14~~]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA~~].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:007473717<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Human rhinovirus b14]]		[[Category: Human rhinovirus b14]]
	[[Category: Hadfield, A.]]		[[Category: Hadfield, A.]]

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

2013-01-04T09:58:03Z

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

←Older revision

Revision as of 09:58, 4 January 2013

OCA at 09:57, 4 January 2013

2013-01-04T09:57:59Z

←Older revision		Revision as of 09:57, 4 January 2013
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-	{{Seed}}
	[[Image:1ruj.png\|left\|200px]]		[[Image:1ruj.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1ruj", 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_1ruj\| PDB=1ruj \| SCENE= }}		{{STRUCTURE_1ruj\| PDB=1ruj \| SCENE= }}

	===RHINOVIRUS 14 MUTANT WITH SER 1 223 REPLACED BY GLY (S1223G)===		===RHINOVIRUS 14 MUTANT WITH SER 1 223 REPLACED BY GLY (S1223G)===

-		+	{{ABSTRACT_PUBMED_7473717}}
-	~~<!--~~	+
-	~~The line below this paragraph,~~ {{~~ABSTRACT_PUBMED_8383239}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 8383239 is the PubMed ID number.~~	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_8383239~~}}	+

	==About this Structure==		==About this Structure==
-	~~1RUJ~~ is a 4 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/~~Human_rhinovirus_14~~ Human rhinovirus 14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA].	+	[[1ruj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_b14 Human rhinovirus b14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUJ OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~8383239~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:007473717</ref><references group="xtra"/>
-	[[Category: Human rhinovirus 14]]	+	[[Category: Human rhinovirus b14]]
	[[Category: Hadfield, A.]]		[[Category: Hadfield, A.]]
	[[Category: Heinz, B A.]]		[[Category: Heinz, B A.]]
Line 37:		Line 25:
	[[Category: Icosahedral virus]]		[[Category: Icosahedral virus]]
	[[Category: Rhinovirus coat protein]]		[[Category: Rhinovirus coat protein]]
-		+	[[Category: Virus]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 17:04:58 2009''~~	+