5wng - Revision history

OCA at 14:16, 13 March 2024

2024-03-13T14:16:34Z

←Older revision		Revision as of 14:16, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='5wng' size='340' side='right'caption='[[5wng]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='5wng' size='340' side='right'caption='[[5wng]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5wng]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WNG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5WNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5wng]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WNG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B4Y:(2R)-N-(3-cyanophenyl)-2-(3-{[(6S)-6-(dimethylamino)-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl]carbamoyl}phenyl)pyrrolidine-1-carboxamide'>B4Y</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]] 2.9Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5wne\|5wne]], [[5wnf\|5wnf]], [[5wnh\|5wnh]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B4Y:(2R)-N-(3-cyanophenyl)-2-(3-{[(6S)-6-(dimethylamino)-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl]carbamoyl}phenyl)pyrrolidine-1-carboxamide'>B4Y</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5wng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wng OCA], [https://pdbe.org/5wng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wng RCSB], [https://www.ebi.ac.uk/pdbsum/5wng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wng ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5wng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wng OCA], [~~http~~://pdbe.org/5wng PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5wng RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5wng PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5wng ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ROCK1_HUMAN ROCK1_HUMAN]] Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation.<ref>PMID:8617235</ref> <ref>PMID:9722579</ref> <ref>PMID:10436159</ref> <ref>PMID:10652353</ref> <ref>PMID:11018042</ref> <ref>PMID:11283607</ref> <ref>PMID:17158456</ref> <ref>PMID:18694941</ref> <ref>PMID:18573880</ref> <ref>PMID:19036714</ref> <ref>PMID:19181962</ref> <ref>PMID:19131646</ref> <ref>PMID:19997641</ref> <ref>PMID:21072057</ref>	+	[https://www.uniprot.org/uniprot/ROCK1_HUMAN ROCK1_HUMAN] Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation.<ref>PMID:8617235</ref> <ref>PMID:9722579</ref> <ref>PMID:10436159</ref> <ref>PMID:10652353</ref> <ref>PMID:11018042</ref> <ref>PMID:11283607</ref> <ref>PMID:17158456</ref> <ref>PMID:18694941</ref> <ref>PMID:18573880</ref> <ref>PMID:19036714</ref> <ref>PMID:19181962</ref> <ref>PMID:19131646</ref> <ref>PMID:19997641</ref> <ref>PMID:21072057</ref>

	==See Also==		==See Also==
-	*[[Rho-associated protein kinase\|Rho-associated protein kinase]]	+	*[[Rho-associated protein kinase 3D structures\|Rho-associated protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Li X]]
-	[[Category: Li, X]]	+
-	~~[[Category: Kinase inhibitor]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Rho kinase]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transferase-inhibitor complex]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 07:13, 7 October 2020

2020-10-07T07:13:26Z

←Older revision		Revision as of 07:13, 7 October 2020
Line 1:		Line 1:

	==X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR==		==X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR==
-	<StructureSection load='5wng' size='340' side='right' caption='[[5wng]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='5wng' size='340' side='right'caption='[[5wng]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5wng]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WNG OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5WNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5wng]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WNG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WNG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B4Y:(2R)-N-(3-cyanophenyl)-2-(3-{[(6S)-6-(dimethylamino)-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl]carbamoyl}phenyl)pyrrolidine-1-carboxamide'>B4Y</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B4Y:(2R)-N-(3-cyanophenyl)-2-(3-{[(6S)-6-(dimethylamino)-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl]carbamoyl}phenyl)pyrrolidine-1-carboxamide'>B4Y</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5wne\|5wne]], [[5wnf\|5wnf]], [[5wnh\|5wnh]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5wne\|5wne]], [[5wnf\|5wnf]], [[5wnh\|5wnh]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5wng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wng OCA], [http://pdbe.org/5wng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wng RCSB], [http://www.ebi.ac.uk/pdbsum/5wng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wng ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wng OCA], [http://pdbe.org/5wng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wng RCSB], [http://www.ebi.ac.uk/pdbsum/5wng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wng ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ROCK1_HUMAN ROCK1_HUMAN]] Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation.<ref>PMID:8617235</ref> <ref>PMID:9722579</ref> <ref>PMID:10436159</ref> <ref>PMID:10652353</ref> <ref>PMID:11018042</ref> <ref>PMID:11283607</ref> <ref>PMID:17158456</ref> <ref>PMID:18694941</ref> <ref>PMID:18573880</ref> <ref>PMID:19036714</ref> <ref>PMID:19181962</ref> <ref>PMID:19131646</ref> <ref>PMID:19997641</ref> <ref>PMID:21072057</ref>		[[http://www.uniprot.org/uniprot/ROCK1_HUMAN ROCK1_HUMAN]] Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation.<ref>PMID:8617235</ref> <ref>PMID:9722579</ref> <ref>PMID:10436159</ref> <ref>PMID:10652353</ref> <ref>PMID:11018042</ref> <ref>PMID:11283607</ref> <ref>PMID:17158456</ref> <ref>PMID:18694941</ref> <ref>PMID:18573880</ref> <ref>PMID:19036714</ref> <ref>PMID:19181962</ref> <ref>PMID:19131646</ref> <ref>PMID:19997641</ref> <ref>PMID:21072057</ref>
		+
		+	==See Also==
		+	*[[Rho-associated protein kinase\|Rho-associated protein kinase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Li, X]]		[[Category: Li, X]]

OCA at 18:37, 1 August 2018

2018-08-01T18:37:28Z

←Older revision		Revision as of 18:37, 1 August 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 5wng is ON HOLD until Paper Publication~~	+	==X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR==
-		+	<StructureSection load='5wng' size='340' side='right' caption='[[5wng]], [[Resolution\|resolution]] 2.90Å' scene=''>
-	~~Authors: Li, X.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5wng]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WNG FirstGlance]. <br>
-	~~Description:~~ X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B4Y:(2R)-N-(3-cyanophenyl)-2-(3-{[(6S)-6-(dimethylamino)-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl]carbamoyl}phenyl)pyrrolidine-1-carboxamide'>B4Y</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5wne\|5wne]], [[5wnf\|5wnf]], [[5wnh\|5wnh]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5wng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wng OCA], [http://pdbe.org/5wng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wng RCSB], [http://www.ebi.ac.uk/pdbsum/5wng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wng ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ROCK1_HUMAN ROCK1_HUMAN]] Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation.<ref>PMID:8617235</ref> <ref>PMID:9722579</ref> <ref>PMID:10436159</ref> <ref>PMID:10652353</ref> <ref>PMID:11018042</ref> <ref>PMID:11283607</ref> <ref>PMID:17158456</ref> <ref>PMID:18694941</ref> <ref>PMID:18573880</ref> <ref>PMID:19036714</ref> <ref>PMID:19181962</ref> <ref>PMID:19131646</ref> <ref>PMID:19997641</ref> <ref>PMID:21072057</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Li, X]]		[[Category: Li, X]]
		+	[[Category: Kinase inhibitor]]
		+	[[Category: Phosphorylation]]
		+	[[Category: Rho kinase]]
		+	[[Category: Transferase]]
		+	[[Category: Transferase-inhibitor complex]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA: Protected "5wng" [edit=sysop:move=sysop]

2017-09-27T15:00:43Z

Protected "5wng" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:00, 27 September 2017

OCA: New page: '''Unreleased structure''' The entry 5wng is ON HOLD until Paper Publication Authors: Li, X. Description: X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELE...

2017-09-27T15:00:42Z

New page: '''Unreleased structure''' The entry 5wng is ON HOLD until Paper Publication Authors: Li, X. Description: X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELE...

New page

'''Unreleased structure'''

The entry 5wng is ON HOLD until Paper Publication

Authors: Li, X.

Description: X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE INHIBITOR
[[Category: Unreleased Structures]]
[[Category: Li, X]]