2vrw - Revision history

OCA at 10:03, 9 May 2024

2024-05-09T10:03:33Z

←Older revision		Revision as of 10:03, 9 May 2024
Line 3:		Line 3:
	<StructureSection load='2vrw' size='340' side='right'caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vrw' size='340' side='right'caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~] and [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRW FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<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]] 1.85Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [https://pdbe.org/2vrw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [https://www.ebi.ac.uk/pdbsum/2vrw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrw 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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [https://pdbe.org/2vrw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [https://www.ebi.ac.uk/pdbsum/2vrw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/RAC1_HUMAN RAC1_HUMAN]] Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> ~~[[https://www.uniprot.org/uniprot/VAV_MOUSE VAV_MOUSE]] Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.~~	+	[https://www.uniprot.org/uniprot/RAC1_HUMAN RAC1_HUMAN] Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Rapley, J]]	+	[[Category: Rapley J]]
-	[[Category: Rittinger, K]]	+	[[Category: Rittinger K]]
-	[[Category: Tybulewicz, V]]	+	[[Category: Tybulewicz V]]
-	~~[[Category: Adp-ribosylation]]~~	+
-	~~[[Category: Exchange factor]]~~	+
-	~~[[Category: Gtp-binding]]~~	+
-	~~[[Category: Gtpase]]~~	+
-	~~[[Category: Guanine-nucleotide releasing factor]]~~	+
-	~~[[Category: Lipoprotein]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Methylation]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Phorbol-ester binding]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Prenylation]]~~	+
-	~~[[Category: Proto-oncogene]]~~	+
-	~~[[Category: Rac]]~~	+
-	~~[[Category: Sh2 domain]]~~	+
-	~~[[Category: Sh3 domain]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Vav]]~~	+
-	~~[[Category: Zinc-finger~~]]	+

OCA at 11:45, 30 March 2022

2022-03-30T11:45:07Z

←Older revision		Revision as of 11:45, 30 March 2022
Line 3:		Line 3:
	<StructureSection load='2vrw' size='340' side='right'caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vrw' size='340' side='right'caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human] and [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2VRW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</div></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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [~~http~~://pdbe.org/2vrw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vrw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrw 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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [https://pdbe.org/2vrw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [https://www.ebi.ac.uk/pdbsum/2vrw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RAC1_HUMAN RAC1_HUMAN]] Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> [[~~http~~://www.uniprot.org/uniprot/VAV_MOUSE VAV_MOUSE]] Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.	+	[[https://www.uniprot.org/uniprot/RAC1_HUMAN RAC1_HUMAN]] Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> [[https://www.uniprot.org/uniprot/VAV_MOUSE VAV_MOUSE]] Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:26, 25 June 2020

2020-06-25T08:26:40Z

←Older revision		Revision as of 08:26, 25 June 2020
Line 1:		Line 1:

	==Critical structural role for the PH and C1 domains of the Vav1 exchange factor==		==Critical structural role for the PH and C1 domains of the Vav1 exchange factor==
-	<StructureSection load='2vrw' size='340' side='right' caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='2vrw' size='340' side='right'caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VRW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VRW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://pdbe.org/2vrw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrw 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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://pdbe.org/2vrw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Rac\|Rac]]	+	*[[Rac 3D structures\|Rac 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Rapley, J]]		[[Category: Rapley, J]]

OCA at 20:43, 19 September 2018

2018-09-19T20:43:06Z

←Older revision		Revision as of 20:43, 19 September 2018
Line 1:		Line 1:

-	==~~CRITICAL STRUCTURAL ROLE FOR THE~~ PH ~~AND~~ C1 ~~DOMAINS OF THE VAV1 EXCHANGE FACTOR~~==	+	==Critical structural role for the PH and C1 domains of the Vav1 exchange factor==
	<StructureSection load='2vrw' size='340' side='right' caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vrw' size='340' side='right' caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vr/2vrw_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vr/2vrw_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 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 2vrw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2vrw" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Rac\|Rac]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 00:10, 5 August 2016

2016-08-05T00:10:17Z

←Older revision		Revision as of 00:10, 5 August 2016
Line 1:		Line 1:
		+
	==CRITICAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE VAV1 EXCHANGE FACTOR==		==CRITICAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE VAV1 EXCHANGE FACTOR==
	<StructureSection load='2vrw' size='340' side='right' caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vrw' size='340' side='right' caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~] and [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VRW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VRW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw 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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://pdbe.org/2vrw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<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=2vrw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	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 2vrw" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Rapley, J]]		[[Category: Rapley, J]]
	[[Category: Rittinger, K]]		[[Category: Rittinger, K]]

OCA at 14:16, 25 December 2014

2014-12-25T14:16:10Z

←Older revision		Revision as of 14:16, 25 December 2014
Line 7:		Line 7:
	<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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw 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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RAC1_HUMAN RAC1_HUMAN]] Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> [[http://www.uniprot.org/uniprot/VAV_MOUSE VAV_MOUSE]] Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Rapley, J.]]	+	[[Category: Rapley, J]]
-	[[Category: Rittinger, K.]]	+	[[Category: Rittinger, K]]
-	[[Category: Tybulewicz, V.]]	+	[[Category: Tybulewicz, V]]
	[[Category: Adp-ribosylation]]		[[Category: Adp-ribosylation]]
	[[Category: Exchange factor]]		[[Category: Exchange factor]]

OCA at 05:56, 10 October 2014

2014-10-10T05:56:13Z

←Older revision		Revision as of 05:56, 10 October 2014
Line 2:		Line 2:
	<StructureSection load='2vrw' size='340' side='right' caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2vrw' size='340' side='right' caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. <br>	+	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VRW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</td></tr>
-	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class~~='~~plainlinks~~'~~>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw PDBsum]</span></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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw PDBsum]</span></td></tr>	+	</table>
-	<table>	+
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 23:
	Crucial structural role for the PH and C1 domains of the Vav1 exchange factor.,Rapley J, Tybulewicz VL, Rittinger K EMBO Rep. 2008 Jul;9(7):655-61. Epub 2008 May 30. PMID:18511940<ref>PMID:18511940</ref>		Crucial structural role for the PH and C1 domains of the Vav1 exchange factor.,Rapley J, Tybulewicz VL, Rittinger K EMBO Rep. 2008 Jul;9(7):655-61. Epub 2008 May 30. PMID:18511940<ref>PMID:18511940</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==

OCA at 08:38, 7 May 2014

2014-05-07T08:38:09Z

←Older revision		Revision as of 08:38, 7 May 2014
Line 1:		Line 1:
-	[[~~Image:~~2vrw.~~png~~\|~~left~~\|200px]]	+	==CRITICAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE VAV1 EXCHANGE FACTOR==
		+	<StructureSection load='2vrw' size='340' side='right' caption='[[2vrw]], [[Resolution\|resolution]] 1.85Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2vrw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e96\|1e96]], [[1i4d\|1i4d]], [[1foe\|1foe]], [[1mh1\|1mh1]], [[1i4l\|1i4l]], [[1he1\|1he1]], [[1ryf\|1ryf]], [[1k1z\|1k1z]], [[1ryh\|1ryh]], [[1hh4\|1hh4]], [[1gcp\|1gcp]], [[1g4u\|1g4u]], [[2fju\|2fju]], [[1f5x\|1f5x]], [[1i4t\|1i4t]], [[1gcq\|1gcq]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=2vrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vrw RCSB], [http://www.ebi.ac.uk/pdbsum/2vrw 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/vr/2vrw_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 Vav family of proteins are guanine nucleotide exchange factors (GEFs) for the Rho family of GTPases, which regulate various cellular functions, including T-cell activation. They contain a catalytic Dbl homology (DH) domain that is invariably followed by a pleckstrin homology (PH) domain, which is often required for catalytic activity. Vav proteins are the first GEFs for which an additional C1 domain is required for full biological activity. Here, we present the structure of a Vav1 fragment comprising the DH-PH-C1 domains bound to Rac1. This structure shows that the PH and C1 domains form a single structural unit that packs against the carboxy-terminal helix of the DH domain to stabilize its conformation and to promote nucleotide exchange. In contrast to previous reports, this structure shows that there are no direct contacts between the GTPase and C1 domain but instead suggests new mechanisms for the regulation of Vav1 activity.

-	~~<!--~~	+	Crucial structural role for the PH and C1 domains of the Vav1 exchange factor.,Rapley J, Tybulewicz VL, Rittinger K EMBO Rep. 2008 Jul;9(7):655-61. Epub 2008 May 30. PMID:18511940<ref>PMID:18511940</ref>
-	~~The line below this paragraph, containing "STRUCTURE_2vrw", 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_2vrw\| PDB=2vrw \| SCENE= }}~~	+

-	~~===CRITICAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE VAV1 EXCHANGE FACTOR===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph~~, ~~{{ABSTRACT_PUBMED_18511940}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 18511940 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_18511940}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2vrw]] is a 2 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:018511940<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

OCA: Protected "2vrw" [edit=sysop:move=sysop]

2011-08-24T05:22:09Z

Protected "2vrw" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:22, 24 August 2011

OCA at 05:22, 24 August 2011

2011-08-24T05:22:08Z

←Older revision		Revision as of 05:22, 24 August 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2vrw.png\|left\|200px]]		[[Image:2vrw.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~2VRW~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA].	+	[[2vrw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRW OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18511940~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018511940</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
Line 30:		Line 29:
	[[Category: Tybulewicz, V.]]		[[Category: Tybulewicz, V.]]
	[[Category: Adp-ribosylation]]		[[Category: Adp-ribosylation]]
-	[[Category: Alternative splicing]]
	[[Category: Exchange factor]]		[[Category: Exchange factor]]
	[[Category: Gtp-binding]]		[[Category: Gtp-binding]]
Line 42:		Line 40:
	[[Category: Phorbol-ester binding]]		[[Category: Phorbol-ester binding]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
-	[[Category: Polymorphism]]
	[[Category: Prenylation]]		[[Category: Prenylation]]
	[[Category: Proto-oncogene]]		[[Category: Proto-oncogene]]
Line 50:		Line 47:
	[[Category: Signaling protein]]		[[Category: Signaling protein]]
	[[Category: Vav]]		[[Category: Vav]]
-	[[Category: Zinc]]
	[[Category: Zinc-finger]]		[[Category: Zinc-finger]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:27:12 2009''