1qjx - Revision history

OCA at 12:47, 13 December 2023

OCA — Wed, 13 Dec 2023 12:47:03 GMT

←Older revision		Revision as of 12:47, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='1qjx' size='340' side='right'caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1qjx' size='340' side='right'caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human_rhinovirus_16 Human rhinovirus 16~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhinovirus_A16 Rhinovirus A16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.8Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [https://pdbe.org/1qjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [https://www.ebi.ac.uk/pdbsum/1qjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjx 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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [https://pdbe.org/1qjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [https://www.ebi.ac.uk/pdbsum/1qjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/POLG_HRV16 POLG_HRV16]] 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. 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 (By similarity). 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_HRV16 POLG_HRV16] 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. 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 (By similarity). 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]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human rhinovirus 16]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Diana, G D]]~~	+	[[Category: Rhinovirus A16]]
-	~~[[Category: Hadfield, A T]]~~	+	[[Category: Diana GD]]
-	~~[[Category: Rossmann, M G]]~~	+	[[Category: Hadfield AT]]
-	~~[[Category: Antiviral compound]]~~	+	[[Category: Rossmann MG]]
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: Capsid protein]]~~	+
-	~~[[Category: Covalent protein-rna linkage]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Cytoplasmic vesicle]]~~	+
-	~~[[Category: Drug]]~~	+
-	~~[[Category: Helicase]]~~	+
-	~~[[Category: Host-virus interaction]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Lipoprotein]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Myristate]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Nucleotidyltransferase]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Protease]]~~	+
-	[[Category: Rhinovirus ~~coat protein~~]]	+
-	[[Category: ~~Rna replication~~]]	+
-	[[Category: ~~Rna-binding~~]]	+
-	[[Category: ~~Rna-directed rna polymerase]]~~	+
-	~~[[Category: Thiol protease]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Virion]]~~	+
-	~~[[Category: Virus]]~~	+
-	~~[[Category: Win compound~~]]	+

OCA at 10:27, 17 February 2021

OCA — Wed, 17 Feb 2021 10:27:56 GMT

←Older revision		Revision as of 10:27, 17 February 2021
Line 3:		Line 3:
	<StructureSection load='1qjx' size='340' side='right'caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1qjx' size='340' side='right'caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human_rhinovirus_16 Human rhinovirus 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1QJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_rhinovirus_16 Human rhinovirus 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [~~http~~://pdbe.org/1qjx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1qjx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjx 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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [https://pdbe.org/1qjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [https://www.ebi.ac.uk/pdbsum/1qjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/POLG_HRV16 POLG_HRV16]] 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. 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 (By similarity). 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_HRV16 POLG_HRV16]] 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. 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 (By similarity). 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 11:41, 10 May 2019

OCA — Fri, 10 May 2019 11:41:50 GMT

←Older revision		Revision as of 11:41, 10 May 2019
Line 1:		Line 1:

	==HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934==		==HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934==
-	<StructureSection load='1qjx' size='340' side='right' caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='1qjx' size='340' side='right'caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_16 Human rhinovirus 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_16 Human rhinovirus 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1qjx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1qjx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Human rhinovirus\|Human rhinovirus]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human rhinovirus 16]]		[[Category: Human rhinovirus 16]]
		+	[[Category: Large Structures]]
	[[Category: Diana, G D]]		[[Category: Diana, G D]]
	[[Category: Hadfield, A T]]		[[Category: Hadfield, A T]]

OCA at 07:55, 24 February 2018

OCA — Sat, 24 Feb 2018 07:55:10 GMT

←Older revision		Revision as of 07:55, 24 February 2018
Line 1:		Line 1:
		+
	==HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934==		==HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934==
	<StructureSection load='1qjx' size='340' side='right' caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1qjx' size='340' side='right' caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Hrv-16 Hrv-~~16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_16 Human rhinovirus 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [http://pdbe.org/1qjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [http://www.ebi.ac.uk/pdbsum/1qjx 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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [http://pdbe.org/1qjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [http://www.ebi.ac.uk/pdbsum/1qjx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/1qjx_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/1qjx_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 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Hrv-~~16]]	+	[[Category: Human rhinovirus 16]]
	[[Category: Diana, G D]]		[[Category: Diana, G D]]
	[[Category: Hadfield, A T]]		[[Category: Hadfield, A T]]
Line 40:		Line 41:
	[[Category: Capsid protein]]		[[Category: Capsid protein]]
	[[Category: Covalent protein-rna linkage]]		[[Category: Covalent protein-rna linkage]]
		+	[[Category: Cytoplasm]]
	[[Category: Cytoplasmic vesicle]]		[[Category: Cytoplasmic vesicle]]
	[[Category: Drug]]		[[Category: Drug]]
	[[Category: Helicase]]		[[Category: Helicase]]
	[[Category: Host-virus interaction]]		[[Category: Host-virus interaction]]
-	[[Category: Human rhinovirus 16]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Lipoprotein]]		[[Category: Lipoprotein]]

OCA at 07:27, 10 February 2016

OCA — Wed, 10 Feb 2016 07:27:20 GMT

←Older revision		Revision as of 07:27, 10 February 2016
Line 17:		Line 17:
	<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=1qjx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:41, 11 September 2015

OCA — Fri, 11 Sep 2015 06:41:22 GMT

←Older revision		Revision as of 06:41, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1qjx' size='340' side='right' caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1qjx' size='340' side='right' caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human_rhinovirus_a16 Human rhinovirus a16~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrv-16 Hrv-16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [http://www.ebi.ac.uk/pdbsum/1qjx 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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [http://pdbe.org/1qjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [http://www.ebi.ac.uk/pdbsum/1qjx PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1qjx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human rhinovirus a16~~]]	+	[[Category: Hrv-16]]
	[[Category: Diana, G D]]		[[Category: Diana, G D]]
	[[Category: Hadfield, A T]]		[[Category: Hadfield, A T]]

OCA at 12:43, 25 December 2014

OCA — Thu, 25 Dec 2014 12:43:18 GMT

←Older revision		Revision as of 12:43, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_a16 Human rhinovirus a16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_a16 Human rhinovirus a16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [http://www.ebi.ac.uk/pdbsum/1qjx 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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [http://www.ebi.ac.uk/pdbsum/1qjx PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLG_HRV16 POLG_HRV16]] 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. 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 (By similarity). 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 30:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Human rhinovirus a16]]		[[Category: Human rhinovirus a16]]
-	[[Category: Diana, G D.]]	+	[[Category: Diana, G D]]
-	[[Category: Hadfield, A T.]]	+	[[Category: Hadfield, A T]]
-	[[Category: Rossmann, M G.]]	+	[[Category: Rossmann, M G]]
	[[Category: Antiviral compound]]		[[Category: Antiviral compound]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]

OCA at 09:44, 3 October 2014

OCA — Fri, 03 Oct 2014 09:44:56 GMT

←Older revision		Revision as of 09:44, 3 October 2014
Line 1:		Line 1:
-	[[~~Image:~~1qjx.~~png~~\|~~left~~\|200px]]	+	==HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934==
		+	<StructureSection load='1qjx' size='340' side='right' caption='[[1qjx]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_a16 Human rhinovirus a16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJX FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=W02:2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL'>W02</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qju\|1qju]], [[1nd3\|1nd3]], [[1aym\|1aym]], [[1ncr\|1ncr]], [[1nd2\|1nd2]], [[1ayn\|1ayn]], [[1c8m\|1c8m]], [[1tp7\|1tp7]], [[1xr7\|1xr7]], [[1d3e\|1d3e]], [[1qjy\|1qjy]], [[1qjz\|1qjz]]</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=1qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qjx RCSB], [http://www.ebi.ac.uk/pdbsum/1qjx 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/qj/1qjx_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 ==
		+	Rhinoviruses are a frequent cause of the common cold. A series of antirhinoviral compounds have been developed that bind into a hydrophobic pocket in the viral capsid, stabilizing the capsid and interfering with cell attachment. The structures of a variety of such compounds, complexed with rhinovirus serotypes 14, 16, 1A, and 3, previously have been examined. Three chemically similar compounds, closely related to a drug that is undergoing phase III clinical trials, were chosen to determine the structural impact of the heteroatoms in one of the three rings. The compounds were found to have binding modes that depend on their electronic distribution. In the compound with the lowest efficacy, the terminal ring is displaced by 1 A and rotated by 180 degrees relative to the structure of the other two. The greater polarity of the terminal ring in one of the three compounds leads to a small displacement of its position relative to the other compounds in the hydrophobic end of the antiviral compound binding pocket to a site where it makes fewer interactions. Its lower efficacy is likely to be the result of the reduced number of interactions. A region of conserved residues has been identified near the entrance to the binding pocket where there is a corresponding conservation of the mode of binding of these compounds to different serotypes. Thus, variations in residues lining the more hydrophobic end of the pocket are primarily responsible for the differences in drug efficacies.

-	~~{{STRUCTURE_1qjx\| PDB=1qjx \| SCENE= }}~~	+	Analysis of three structurally related antiviral compounds in complex with human rhinovirus 16.,Hadfield AT, Diana GD, Rossmann MG Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14730-5. PMID:10611281<ref>PMID:10611281</ref>

-	~~===HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_10611281}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1qjx]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Human_rhinovirus_a16 Human rhinovirus a16]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:010611281<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Human rhinovirus a16]]		[[Category: Human rhinovirus a16]]
	[[Category: Diana, G D.]]		[[Category: Diana, G D.]]

OCA at 09:30, 16 January 2013

OCA — Wed, 16 Jan 2013 09:30:16 GMT

←Older revision		Revision as of 09:30, 16 January 2013
Line 1:		Line 1:
	[[Image:1qjx.png\|left\|200px]]		[[Image:1qjx.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1qjx", 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_1qjx\| PDB=1qjx \| SCENE= }}		{{STRUCTURE_1qjx\| PDB=1qjx \| SCENE= }}

	===HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934===		===HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_10611281}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 10611281 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_10611281}}		{{ABSTRACT_PUBMED_10611281}}

	==About this Structure==		==About this Structure==
-	[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human_rhinovirus_16~~ Human rhinovirus 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA].	+	[[1qjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_a16 Human rhinovirus a16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJX OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:10611281</ref><ref group="xtra">PMID:9083115</ref><ref group="xtra">PMID:7915182</ref><ref group="xtra">PMID:8383771</ref><ref group="xtra">PMID:2555523</ref><ref group="xtra">PMID:3018924</ref><ref group="xtra">PMID:2993920</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010611281</ref><references group="xtra"/>
-	[[Category: Human rhinovirus 16]]	+	[[Category: Human rhinovirus a16]]
	[[Category: Diana, G D.]]		[[Category: Diana, G D.]]
	[[Category: Hadfield, A T.]]		[[Category: Hadfield, A T.]]
Line 31:		Line 20:
	[[Category: Capsid protein]]		[[Category: Capsid protein]]
	[[Category: Covalent protein-rna linkage]]		[[Category: Covalent protein-rna linkage]]
-	[[Category: Cytoplasm]]
	[[Category: Cytoplasmic vesicle]]		[[Category: Cytoplasmic vesicle]]
	[[Category: Drug]]		[[Category: Drug]]

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

OCA — Mon, 14 Mar 2011 23:14:21 GMT

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

←Older revision

Revision as of 23:14, 14 March 2011