5m70 - Revision history

OCA at 18:28, 1 November 2023

2023-11-01T18:28:06Z

←Older revision		Revision as of 18:28, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='5m70' size='340' side='right'caption='[[5m70]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5m70' size='340' side='right'caption='[[5m70]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5m70]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M70 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5M70 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5m70]] 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=5M70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M70 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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]] 2.2Å</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=5m70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m70 OCA], [~~http~~://pdbe.org/5m70 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5m70 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5m70 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5m70 ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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'>[https://proteopedia.org/fgij/fg.htm?mol=5m70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m70 OCA], [https://pdbe.org/5m70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m70 RCSB], [https://www.ebi.ac.uk/pdbsum/5m70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m70 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/RHG01_HUMAN RHG01_HUMAN]] GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate. [[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>	+	[https://www.uniprot.org/uniprot/RHG01_HUMAN RHG01_HUMAN] GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bowler~~, M W~~]]	+	[[Category: Bowler MW]]
-	[[Category: Pellegrini, E]]	+	[[Category: Pellegrini E]]
-	~~[[Category: Arginine finger]]~~	+
-	~~[[Category: Rhoa]]~~	+
-	~~[[Category: Rhogap]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Transition state~~]]	+

OCA at 07:09, 19 August 2020

2020-08-19T07:09:52Z

←Older revision		Revision as of 07:09, 19 August 2020
Line 1:		Line 1:

	==Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in complex with RhoA.GDP.AlF4- human==		==Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in complex with RhoA.GDP.AlF4- human==
-	<StructureSection load='5m70' size='340' side='right' caption='[[5m70]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='5m70' size='340' side='right'caption='[[5m70]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5m70]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M70 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5M70 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5m70]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M70 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M70 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5m70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m70 OCA], [http://pdbe.org/5m70 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m70 RCSB], [http://www.ebi.ac.uk/pdbsum/5m70 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m70 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=5m70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m70 OCA], [http://pdbe.org/5m70 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m70 RCSB], [http://www.ebi.ac.uk/pdbsum/5m70 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m70 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 5m70" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5m70" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Rho GTPase 3D structures\|Rho GTPase 3D structures]]
		+	*[[Rho GTPase activating protein 3D structures\|Rho GTPase activating protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Bowler, M W]]		[[Category: Bowler, M W]]
	[[Category: Pellegrini, E]]		[[Category: Pellegrini, E]]

OCA at 03:54, 6 September 2017

2017-09-06T03:54:33Z

←Older revision		Revision as of 03:54, 6 September 2017
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/RHG01_HUMAN RHG01_HUMAN]] GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate. [[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/RHG01_HUMAN RHG01_HUMAN]] GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate. [[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	We report X-ray crystallographic and 19 F NMR studies of the G-protein RhoA complexed with MgF3- , GDP, and RhoGAP, which has the mutation Arg85'Ala. When combined with DFT calculations, these data permit the identification of changes in transition state (TS) properties. The X-ray data show how Tyr34 maintains solvent exclusion and the core H-bond network in the active site by relocating to replace the missing Arg85' sidechain. The 19 F NMR data show deshielding effects that indicate the main function of Arg85' is electronic polarization of the transferring phosphoryl group, primarily mediated by H-bonding to O3G and thence to PG . DFT calculations identify electron-density redistribution and pinpoint why the TS for guanosine 5'-triphosphate (GTP) hydrolysis is higher in energy when RhoA is complexed with RhoGAPArg85'Ala relative to wild-type (WT) RhoGAP. This study demonstrates that 19 F NMR measurements, in combination with X-ray crystallography and DFT calculations, can reliably dissect the response of small GTPases to site-specific modifications.
		+
		+	Assessing the Influence of Mutation on GTPase Transition States by Using X-ray Crystallography, 19 F NMR, and DFT Approaches.,Jin Y, Molt RW Jr, Pellegrini E, Cliff MJ, Bowler MW, Richards NGJ, Blackburn GM, Waltho JP Angew Chem Int Ed Engl. 2017 Aug 7;56(33):9732-9735. doi: 10.1002/anie.201703074., Epub 2017 May 24. PMID:28498638<ref>PMID:28498638</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5m70" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:48, 17 May 2017

2017-05-17T15:48:02Z

←Older revision		Revision as of 15:48, 17 May 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 5m70 is ON HOLD until Paper Publication~~	+	==Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in complex with RhoA.GDP.AlF4- human==
-		+	<StructureSection load='5m70' size='340' side='right' caption='[[5m70]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~Authors: Pellegrini, E., Bowler, M.W.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5m70]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M70 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M70 FirstGlance]. <br>
-	~~Description:~~ Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in complex with RhoA.GDP.AlF4-human	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<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=5m70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m70 OCA], [http://pdbe.org/5m70 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m70 RCSB], [http://www.ebi.ac.uk/pdbsum/5m70 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m70 ProSAT]</span></td></tr>
-	[[Category: Bowler, M.W]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RHG01_HUMAN RHG01_HUMAN]] GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate. [[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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bowler, M W]]
	[[Category: Pellegrini, E]]		[[Category: Pellegrini, E]]
		+	[[Category: Arginine finger]]
		+	[[Category: Rhoa]]
		+	[[Category: Rhogap]]
		+	[[Category: Signaling protein]]
		+	[[Category: Transition state]]

OCA at 16:26, 9 December 2016

2016-12-09T16:26:47Z

←Older revision		Revision as of 16:26, 9 December 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5m70 is ON HOLD	+	The entry 5m70 is ON HOLD until Paper Publication

	Authors: Pellegrini, E., Bowler, M.W.		Authors: Pellegrini, E., Bowler, M.W.

OCA: Protected "5m70" [edit=sysop:move=sysop]

2016-11-02T16:04:57Z

Protected "5m70" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:04, 2 November 2016

OCA: New page: '''Unreleased structure''' The entry 5m70 is ON HOLD Authors: Pellegrini, E., Bowler, M.W. Description: Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in comple...

2016-11-02T16:04:56Z

New page: '''Unreleased structure''' The entry 5m70 is ON HOLD Authors: Pellegrini, E., Bowler, M.W. Description: Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in comple...

New page

'''Unreleased structure'''

The entry 5m70 is ON HOLD

Authors: Pellegrini, E., Bowler, M.W.

Description: Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in complex with RhoA.GDP.AlF4-human
[[Category: Unreleased Structures]]
[[Category: Bowler, M.W]]
[[Category: Pellegrini, E]]