1s1c - Revision history

OCA at 08:27, 14 February 2024

OCA — Wed, 14 Feb 2024 08:27:28 GMT

←Older revision		Revision as of 08:27, 14 February 2024
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	<StructureSection load='1s1c' size='340' side='right'caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='1s1c' size='340' side='right'caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1s1c]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1S1C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1s1c]] 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=1S1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S1C FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID~~-~~GUANYLATE+ESTER'>GNP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.6Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~ARHA, ARH12, RHOA, RHO12 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [~~http~~://pdbe.org/1s1c PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1s1c PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1c 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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [https://pdbe.org/1s1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [https://www.ebi.ac.uk/pdbsum/1s1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1c ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/RHOA_HUMAN RHOA_HUMAN]] Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.<ref>PMID:8910519</ref> <ref>PMID:9121475</ref> <ref>PMID:12900402</ref> <ref>PMID:16103226</ref> <ref>PMID:16236794</ref> <ref>PMID:19934221</ref> <ref>PMID:20937854</ref> <ref>PMID:20974804</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>	+	[https://www.uniprot.org/uniprot/RHOA_HUMAN RHOA_HUMAN] Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.<ref>PMID:8910519</ref> <ref>PMID:9121475</ref> <ref>PMID:12900402</ref> <ref>PMID:16103226</ref> <ref>PMID:16236794</ref> <ref>PMID:19934221</ref> <ref>PMID:20937854</ref> <ref>PMID:20974804</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</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=1s1c 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=1s1c ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The Rho-ROCK pathway modulates the phosphorylation level of a variety of important signaling proteins and is thereby involved in miscellaneous cellular processes including cell migration, neurite outgrowth, and smooth muscle contraction. The observation of the involvement of the Rho-ROCK pathway in tumor invasion and in diseases such as hypertension and bronchial asthma makes it an interesting target for drug development. We herein present the crystal structure of the complex between active RhoA and the Rho-binding domain of ROCKI. The Rho-binding domain structure forms a parallel alpha-helical coiled-coil dimer and, in contrast to the published Rho-protein kinase N structure, binds exclusively to the switch I and II regions of the guanosine 5'-(beta,gamma-imido)triphosphate-bound RhoA. The switch regions of two different RhoA molecules form a predominantly hydrophobic patch, which is complementarily bound by two identical short helices of 13 residues (amino acids 998-1010). The identified ROCK-binding site of RhoA strikingly supports the assumption of a common consensus-binding site for effector recognition.
-
-	Structural insights into the interaction of ROCKI with the switch regions of RhoA.,Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR J Biol Chem. 2004 Feb 20;279(8):7098-104. Epub 2003 Dec 2. PMID:14660612<ref>PMID:14660612</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1s1c" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Rho GTPase 3D structures\|Rho GTPase 3D structures]]		*[[Rho GTPase 3D structures\|Rho GTPase 3D structures]]
-	*[[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: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ahmadian~~, M R~~]]	+	[[Category: Ahmadian MR]]
-	[[Category: Blumenstein, L]]	+	[[Category: Blumenstein L]]
-	[[Category: Dvorsky, R]]	+	[[Category: Dvorsky R]]
-	[[Category: Vetter~~, I R]]~~	+	[[Category: Vetter IR]]
-	~~[[Category: Coiled-coil]]~~	+
-	~~[[Category: Gtpase]]~~	+
-	~~[[Category: Rho kinase]]~~	+
-	~~[[Category: Rock]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 13:38, 16 December 2020

OCA — Wed, 16 Dec 2020 13:38:01 GMT

←Older revision		Revision as of 13:38, 16 December 2020
Line 1:		Line 1:

	==Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI==		==Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI==
-	<StructureSection load='1s1c' size='340' side='right' caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='1s1c' size='340' side='right'caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1s1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1S1C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1s1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S1C FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://pdbe.org/1s1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1c 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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://pdbe.org/1s1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1c ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Rho GTPase\|Rho GTPase]]	+	*[[Rho GTPase 3D structures\|Rho GTPase 3D structures]]
	*[[Rho-associated protein kinase\|Rho-associated protein kinase]]		*[[Rho-associated protein kinase\|Rho-associated protein kinase]]
	== References ==		== References ==
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ahmadian, M R]]		[[Category: Ahmadian, M R]]
	[[Category: Blumenstein, L]]		[[Category: Blumenstein, L]]

OCA at 06:46, 8 March 2018

OCA — Thu, 08 Mar 2018 06:46:13 GMT

←Older revision		Revision as of 06:46, 8 March 2018
Line 1:		Line 1:
		+
	==Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI==		==Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI==
	<StructureSection load='1s1c' size='340' side='right' caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='1s1c' size='340' side='right' caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://pdbe.org/1s1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c 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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://pdbe.org/1s1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1c 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/s1/1s1c_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s1/1s1c_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=1s1c ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1s1c" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1s1c" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Rho GTPase\|Rho GTPase]]
		+	*[[Rho-associated protein kinase\|Rho-associated protein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:41, 11 September 2015

OCA — Fri, 11 Sep 2015 16:41:03 GMT

←Older revision		Revision as of 16:41, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1s1c' size='340' side='right' caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='1s1c' size='340' side='right' caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1s1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S1C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1s1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S1C FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c 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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://pdbe.org/1s1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c 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 1s1c" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Ahmadian, M R]]		[[Category: Ahmadian, M R]]
	[[Category: Blumenstein, L]]		[[Category: Blumenstein, L]]

OCA at 19:08, 25 December 2014

OCA — Thu, 25 Dec 2014 19:08:10 GMT

←Older revision		Revision as of 19:08, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1s1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S1C FirstGlance]. <br>		<table><tr><td colspan='2'>[[1s1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S1C FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c 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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RHOA_HUMAN RHOA_HUMAN]] Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.<ref>PMID:8910519</ref> <ref>PMID:9121475</ref> <ref>PMID:12900402</ref> <ref>PMID:16103226</ref> <ref>PMID:16236794</ref> <ref>PMID:19934221</ref> <ref>PMID:20937854</ref> <ref>PMID:20974804</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>
	== 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: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Ahmadian, M R.]]	+	[[Category: Ahmadian, M R]]
-	[[Category: Blumenstein, L.]]	+	[[Category: Blumenstein, L]]
-	[[Category: Dvorsky, R.]]	+	[[Category: Dvorsky, R]]
-	[[Category: Vetter, I R.]]	+	[[Category: Vetter, I R]]
	[[Category: Coiled-coil]]		[[Category: Coiled-coil]]
	[[Category: Gtpase]]		[[Category: Gtpase]]

OCA at 13:58, 29 September 2014

OCA — Mon, 29 Sep 2014 13:58:05 GMT

←Older revision		Revision as of 13:58, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1s1c.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI==
		+	<StructureSection load='1s1c' size='340' side='right' caption='[[1s1c]], [[Resolution\|resolution]] 2.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1s1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S1C FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHA, ARH12, RHOA, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=1s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s1c RCSB], [http://www.ebi.ac.uk/pdbsum/1s1c 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/s1/1s1c_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 ==
		+	The Rho-ROCK pathway modulates the phosphorylation level of a variety of important signaling proteins and is thereby involved in miscellaneous cellular processes including cell migration, neurite outgrowth, and smooth muscle contraction. The observation of the involvement of the Rho-ROCK pathway in tumor invasion and in diseases such as hypertension and bronchial asthma makes it an interesting target for drug development. We herein present the crystal structure of the complex between active RhoA and the Rho-binding domain of ROCKI. The Rho-binding domain structure forms a parallel alpha-helical coiled-coil dimer and, in contrast to the published Rho-protein kinase N structure, binds exclusively to the switch I and II regions of the guanosine 5'-(beta,gamma-imido)triphosphate-bound RhoA. The switch regions of two different RhoA molecules form a predominantly hydrophobic patch, which is complementarily bound by two identical short helices of 13 residues (amino acids 998-1010). The identified ROCK-binding site of RhoA strikingly supports the assumption of a common consensus-binding site for effector recognition.

-	~~{{STRUCTURE_1s1c\| PDB=1s1c \| SCENE= }}~~	+	Structural insights into the interaction of ROCKI with the switch regions of RhoA.,Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR J Biol Chem. 2004 Feb 20;279(8):7098-104. Epub 2003 Dec 2. PMID:14660612<ref>PMID:14660612</ref>

-	~~===Crystal structure~~ of the ~~complex between the human RhoA and Rho-binding domain of human ROCKI===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14660612}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1s1c]] is a 4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:014660612<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ahmadian, M R.]]		[[Category: Ahmadian, M R.]]

OCA: Protected "1s1c" [edit=sysop:move=sysop]

OCA — Fri, 04 Jan 2013 10:12:26 GMT

Protected "1s1c" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:12, 4 January 2013

OCA at 10:12, 4 January 2013

OCA — Fri, 04 Jan 2013 10:12:24 GMT

←Older revision		Revision as of 10:12, 4 January 2013
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-	{{Seed}}
	[[Image:1s1c.png\|left\|200px]]		[[Image:1s1c.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1s1c", 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_1s1c\| PDB=1s1c \| SCENE= }}		{{STRUCTURE_1s1c\| PDB=1s1c \| SCENE= }}

	===Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI===		===Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_14660612}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 14660612 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_14660612}}		{{ABSTRACT_PUBMED_14660612}}

	==About this Structure==		==About this Structure==
-	~~1S1C~~ is a 4 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA].	+	[[1s1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~14660612~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:014660612</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ahmadian, M R.]]		[[Category: Ahmadian, M R.]]
Line 33:		Line 21:
	[[Category: Rho kinase]]		[[Category: Rho kinase]]
	[[Category: Rock]]		[[Category: Rock]]
-		+	[[Category: Signaling protein]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Wed Feb 18 04:00:43 2009''~~	+

OCA at 02:00, 18 February 2009

OCA — Wed, 18 Feb 2009 02:00:44 GMT

←Older revision		Revision as of 02:00, 18 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	1S1C is a ~~[[Protein complex]]~~ structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA].	+	1S1C is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1C OCA].

	==Reference==		==Reference==
-	~~Structural insights into the interaction of ROCKI with the switch regions of RhoA., Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR, J Biol Chem. 2004 Feb 20;279(8):7098-104. Epub 2003 Dec 2.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/14660612 14660612]~~	+	<ref group="xtra">PMID:14660612</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Protein complex]]
	[[Category: Ahmadian, M R.]]		[[Category: Ahmadian, M R.]]
	[[Category: Blumenstein, L.]]		[[Category: Blumenstein, L.]]
Line 35:		Line 34:
	[[Category: Rock]]		[[Category: Rock]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 10~~:11:~~24 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:00:43 2009''

OCA at 07:11, 29 July 2008

OCA — Tue, 29 Jul 2008 07:11:27 GMT

←Older revision		Revision as of 07:11, 29 July 2008
Line 1:		Line 1:
-	[[Image:1s1c.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1s1c.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_1s1c\| PDB=1s1c \| SCENE= }}		{{STRUCTURE_1s1c\| PDB=1s1c \| SCENE= }}

-	~~'''~~Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI~~'''~~	+	===Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI===


-	~~==Overview==~~	+	<!--
-	The ~~Rho-ROCK pathway modulates the phosphorylation level of a variety of important signaling proteins and is thereby involved in miscellaneous cellular processes including cell migration~~, ~~neurite outgrowth~~, ~~and smooth muscle contraction. The observation of~~ the ~~involvement of~~ the ~~Rho-ROCK pathway in tumor invasion and in diseases such~~ as ~~hypertension and bronchial asthma makes~~ it ~~an interesting target for drug development~~. ~~We herein present the crystal structure of the complex between active RhoA and the Rho-binding domain of ROCKI~~. The Rho-binding domain structure forms a parallel alpha-helical coiled-coil dimer and, in contrast to the published Rho-protein kinase N structure, binds exclusively to the switch I and II regions of the guanosine 5'-(beta,gamma-imido)~~triphosphate-bound RhoA. The switch regions of two different RhoA molecules form a predominantly hydrophobic patch~~, ~~which~~ is ~~complementarily bound by two identical short helices of 13 residues (amino acids 998-1010)~~. ~~The identified ROCK~~-~~binding site of RhoA strikingly supports the assumption of a common consensus~~-~~binding site for effector recognition.~~	+	The line below this paragraph, {{ABSTRACT_PUBMED_14660612}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 14660612 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_14660612}}

	==About this Structure==		==About this Structure==
Line 30:		Line 34:
	[[Category: Rho kinase]]		[[Category: Rho kinase]]
	[[Category: Rock]]		[[Category: Rock]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 08:~~10:09 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:11:24 2008''