3fg7 - Revision history

OCA at 06:45, 6 September 2023

2023-09-06T06:45:55Z

←Older revision		Revision as of 06:45, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3fg7' size='340' side='right'caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3fg7' size='340' side='right'caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fg7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fg7]] is a 2 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=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1yu5\|1yu5]], [[1p8x\|1p8x]], [[1nph\|1nph]]</div></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]] 2Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">VIL, VIL1 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [https://pdbe.org/3fg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [https://www.ebi.ac.uk/pdbsum/3fg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fg7 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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [https://pdbe.org/3fg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [https://www.ebi.ac.uk/pdbsum/3fg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fg7 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.	+	[https://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>PMID:3087992</ref> <ref>PMID:11500485</ref> <ref>PMID:14594952</ref> <ref>PMID:15084600</ref> <ref>PMID:15272027</ref> <ref>PMID:15342783</ref> <ref>PMID:16921170</ref> <ref>PMID:17229814</ref> <ref>PMID:17606613</ref> <ref>PMID:17182858</ref> <ref>PMID:18054784</ref> <ref>PMID:18198174</ref> <ref>PMID:19808673</ref>	+	[https://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>PMID:3087992</ref> <ref>PMID:11500485</ref> <ref>PMID:14594952</ref> <ref>PMID:15084600</ref> <ref>PMID:15272027</ref> <ref>PMID:15342783</ref> <ref>PMID:16921170</ref> <ref>PMID:17229814</ref> <ref>PMID:17606613</ref> <ref>PMID:17182858</ref> <ref>PMID:18054784</ref> <ref>PMID:18198174</ref> <ref>PMID:19808673</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Burtnick~~, L D~~]]	+	[[Category: Burtnick LD]]
-	[[Category: Robinson~~, R C~~]]	+	[[Category: Robinson RC]]
-	[[Category: Wang, H]]	+	[[Category: Wang H]]
-	~~[[Category: Actin binding protein]]~~	+
-	~~[[Category: Actin capping]]~~	+
-	~~[[Category: Actin-binding]]~~	+
-	~~[[Category: Calcium]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Cytoskeleton]]~~	+
-	~~[[Category: Gelsolin]]~~	+
-	~~[[Category: Structural protein]]~~	+
-	~~[[Category: Villin]]~~	+
-	~~[[Category: Villin head piece~~]]	+

OCA at 08:00, 2 March 2022

2022-03-02T08:00:42Z

←Older revision		Revision as of 08:00, 2 March 2022
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	==The crystal structure of villin domain 6==		==The crystal structure of villin domain 6==
-	<StructureSection load='3fg7' size='340' side='right' caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='3fg7' size='340' side='right'caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fg7]] is a 2 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=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fg7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yu5\|1yu5]], [[1p8x\|1p8x]], [[1nph\|1nph]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yu5\|1yu5]], [[1p8x\|1p8x]], [[1nph\|1nph]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VIL, VIL1 ([~~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">VIL, VIL1 ([https://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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [~~http~~://pdbe.org/3fg7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3fg7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3fg7 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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [https://pdbe.org/3fg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [https://www.ebi.ac.uk/pdbsum/3fg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fg7 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.	+	[[https://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>PMID:3087992</ref> <ref>PMID:11500485</ref> <ref>PMID:14594952</ref> <ref>PMID:15084600</ref> <ref>PMID:15272027</ref> <ref>PMID:15342783</ref> <ref>PMID:16921170</ref> <ref>PMID:17229814</ref> <ref>PMID:17606613</ref> <ref>PMID:17182858</ref> <ref>PMID:18054784</ref> <ref>PMID:18198174</ref> <ref>PMID:19808673</ref>	+	[[https://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>PMID:3087992</ref> <ref>PMID:11500485</ref> <ref>PMID:14594952</ref> <ref>PMID:15084600</ref> <ref>PMID:15272027</ref> <ref>PMID:15342783</ref> <ref>PMID:16921170</ref> <ref>PMID:17229814</ref> <ref>PMID:17606613</ref> <ref>PMID:17182858</ref> <ref>PMID:18054784</ref> <ref>PMID:18198174</ref> <ref>PMID:19808673</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/3fg7_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/3fg7_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 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3fg7" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3fg7" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Villin\|Villin]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Burtnick, L D]]		[[Category: Burtnick, L D]]
	[[Category: Robinson, R C]]		[[Category: Robinson, R C]]

OCA at 06:41, 1 November 2017

2017-11-01T06:41:48Z

←Older revision		Revision as of 06:41, 1 November 2017
Line 1:		Line 1:
		+
	==The crystal structure of villin domain 6==		==The crystal structure of villin domain 6==
	<StructureSection load='3fg7' size='340' side='right' caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3fg7' size='340' side='right' caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yu5\|1yu5]], [[1p8x\|1p8x]], [[1nph\|1nph]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yu5\|1yu5]], [[1p8x\|1p8x]], [[1nph\|1nph]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VIL, VIL1 ([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">VIL, VIL1 ([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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [http://pdbe.org/3fg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg7 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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [http://pdbe.org/3fg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fg7 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3fg7" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3fg7" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Villin\|Villin]]
	== References ==		== References ==
	<references/>		<references/>
Line 44:		Line 42:
	[[Category: Actin capping]]		[[Category: Actin capping]]
	[[Category: Actin-binding]]		[[Category: Actin-binding]]
		+	[[Category: Calcium]]
		+	[[Category: Cytoplasm]]
	[[Category: Cytoskeleton]]		[[Category: Cytoskeleton]]
	[[Category: Gelsolin]]		[[Category: Gelsolin]]

OCA at 23:58, 9 February 2016

2016-02-09T23:58:49Z

←Older revision		Revision as of 23:58, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='3fg7' size='340' side='right' caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3fg7' size='340' side='right' caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fg7]] is a 2 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=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fg7]] is a 2 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=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yu5\|1yu5]], [[1p8x\|1p8x]], [[1nph\|1nph]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yu5\|1yu5]], [[1p8x\|1p8x]], [[1nph\|1nph]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VIL, VIL1 ([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">VIL, VIL1 ([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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg7 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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [http://pdbe.org/3fg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg7 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 19:
	<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=3fg7 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	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 3fg7" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Burtnick, L D]]		[[Category: Burtnick, L D]]
	[[Category: Robinson, R C]]		[[Category: Robinson, R C]]

OCA at 13:54, 18 December 2014

2014-12-18T13:54:11Z

←Older revision		Revision as of 13:54, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3fg7\| PDB=3fg7 \| SCENE= }}~~	+	==The crystal structure of villin domain 6==
-	===The crystal structure of villin domain 6===	+	<StructureSection load='3fg7' size='340' side='right' caption='[[3fg7]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19491107}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3fg7]] is a 2 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=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yu5\|1yu5]], [[1p8x\|1p8x]], [[1nph\|1nph]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VIL, VIL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg7 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.		[[http://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>PMID:3087992</ref> <ref>PMID:11500485</ref> <ref>PMID:14594952</ref> <ref>PMID:15084600</ref> <ref>PMID:15272027</ref> <ref>PMID:15342783</ref> <ref>PMID:16921170</ref> <ref>PMID:17229814</ref> <ref>PMID:17606613</ref> <ref>PMID:17182858</ref> <ref>PMID:18054784</ref> <ref>PMID:18198174</ref> <ref>PMID:19808673</ref>
		+	== 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/fg/3fg7_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 ==
		+	Villin and gelsolin consist of six homologous domains of the gelsolin/cofilin fold (V1-V6 and G1-G6, respectively). Villin differs from gelsolin in possessing at its C terminus an unrelated seventh domain, the villin headpiece. Here, we present the crystal structure of villin domain V6 in an environment in which intact villin would be inactive, in the absence of bound Ca(2+) or phosphorylation. The structure of V6 more closely resembles that of the activated form of G6, which contains one bound Ca(2+), rather than that of the calcium ion-free form of G6 within intact inactive gelsolin. Strikingly apparent is that the long helix in V6 is straight, as found in the activated form of G6, as opposed to the kinked version in inactive gelsolin. Molecular dynamics calculations suggest that the preferable conformation for this helix in the isolated G6 domain is also straight in the absence of Ca(2+) and other gelsolin domains. However, the G6 helix bends in intact calcium ion-free gelsolin to allow interaction with G2 and G4. We suggest that a similar situation exists in villin. Within the intact protein, a bent V6 helix, when triggered by Ca(2+), straightens and helps push apart adjacent domains to expose actin-binding sites within the protein. The sixth domain in this superfamily of proteins serves as a keystone that locks together a compact ensemble of domains in an inactive state. Perturbing the keystone initiates reorganization of the structure to reveal previously buried actin-binding sites.

-	~~==Function==~~	+	Helix straightening as an activation mechanism in the gelsolin superfamily of actin regulatory proteins.,Wang H, Chumnarnsilpa S, Loonchanta A, Li Q, Kuan YM, Robine S, Larsson M, Mihalek I, Burtnick LD, Robinson RC J Biol Chem. 2009 Aug 7;284(32):21265-9. Epub 2009 Jun 1. PMID:19491107<ref>PMID:19491107</ref>
-	~~[[http://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates~~ the ~~reorganization~~ of ~~microvillar~~ actin ~~filaments~~. ~~Plays a role in the actin nucleation~~, ~~actin filament bundle assembly~~, ~~actin filament capping and severing. Binds phosphatidylinositol 4~~,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, ~~cell invasion~~, ~~cell migration and apoptosis~~. ~~Protects against apoptosis induced by dextran sodium sulfate~~ (~~DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF~~)-~~induced epithelial cell motility, chemotaxis and wound repair~~. ~~Upon S~~.~~flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>~~PMID:3087992</ref><ref>PMID:11500485</ref><ref>PMID:14594952</ref><ref>PMID:15084600</ref><ref>PMID:15272027</ref><ref>PMID:15342783</ref><ref>PMID:16921170</ref><ref>PMID:17229814</ref><ref>PMID:17606613</ref><ref>PMID:17182858</ref><ref>PMID:18054784</ref><ref>PMID:18198174</ref><ref>PMID:~~19808673~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3fg7]] is~~ a ~~2 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=3FG7 OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Villin\|Villin]]		*[[Villin\|Villin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019491107</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Burtnick, L D.]]	+	[[Category: Burtnick, L D]]
-	[[Category: Robinson, R C.]]	+	[[Category: Robinson, R C]]
-	[[Category: Wang, H.]]	+	[[Category: Wang, H]]
	[[Category: Actin binding protein]]		[[Category: Actin binding protein]]
	[[Category: Actin capping]]		[[Category: Actin capping]]

OCA at 21:02, 24 March 2013

2013-03-24T21:02:12Z

←Older revision		Revision as of 21:02, 24 March 2013
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-	[[Image:3fg7.png\|left\|200px]]
-
	{{STRUCTURE_3fg7\| PDB=3fg7 \| SCENE= }}		{{STRUCTURE_3fg7\| PDB=3fg7 \| SCENE= }}
-
	===The crystal structure of villin domain 6===		===The crystal structure of villin domain 6===
		+	{{ABSTRACT_PUBMED_19491107}}

-	~~{{ABSTRACT_PUBMED_19491107}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>PMID:3087992</ref><ref>PMID:11500485</ref><ref>PMID:14594952</ref><ref>PMID:15084600</ref><ref>PMID:15272027</ref><ref>PMID:15342783</ref><ref>PMID:16921170</ref><ref>PMID:17229814</ref><ref>PMID:17606613</ref><ref>PMID:17182858</ref><ref>PMID:18054784</ref><ref>PMID:18198174</ref><ref>PMID:19808673</ref>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019491107</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019491107</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burtnick, L D.]]		[[Category: Burtnick, L D.]]

OCA at 15:35, 20 October 2012

2012-10-20T15:35:43Z

←Older revision		Revision as of 15:35, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3fg7]] is a 2 chain structure ~~of [[Villin]]~~ 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=3FG7 OCA].	+	[[3fg7]] is a 2 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=3FG7 OCA].

	==See Also==		==See Also==

OCA: Protected "3fg7" [edit=sysop:move=sysop]

2012-07-26T18:52:45Z

Protected "3fg7" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:52, 26 July 2012

OCA at 18:52, 26 July 2012

2012-07-26T18:52:44Z

←Older revision		Revision as of 18:52, 26 July 2012
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-	{{Seed}}
	[[Image:3fg7.png\|left\|200px]]		[[Image:3fg7.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3fg7", 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_3fg7\| PDB=3fg7 \| SCENE= }}		{{STRUCTURE_3fg7\| PDB=3fg7 \| SCENE= }}

	===The crystal structure of villin domain 6===		===The crystal structure of villin domain 6===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19491107}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19491107 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_19491107}}		{{ABSTRACT_PUBMED_19491107}}

	==About this Structure==		==About this Structure==
-	~~3FG7~~ is a 2 ~~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=3FG7 OCA].	+	[[3fg7]] is a 2 chain structure of [[Villin]] 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=3FG7 OCA].
		+
		+	==See Also==
		+	*[[Villin\|Villin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19491107~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019491107</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burtnick, L D.]]		[[Category: Burtnick, L D.]]
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	[[Category: Actin capping]]		[[Category: Actin capping]]
	[[Category: Actin-binding]]		[[Category: Actin-binding]]
-	[[Category: Calcium]]
-	[[Category: Cytoplasm]]
	[[Category: Cytoskeleton]]		[[Category: Cytoskeleton]]
	[[Category: Gelsolin]]		[[Category: Gelsolin]]
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	[[Category: Villin]]		[[Category: Villin]]
	[[Category: Villin head piece]]		[[Category: Villin head piece]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 12 12:37:23 2009''

OCA at 09:37, 12 August 2009

2009-08-12T09:37:24Z

←Older revision		Revision as of 09:37, 12 August 2009
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	{{Seed}}		{{Seed}}
-	[[Image:3fg7.~~jpg~~\|left\|200px]]	+	[[Image:3fg7.png\|left\|200px]]

	<!--		<!--
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	===The crystal structure of villin domain 6===		===The crystal structure of villin domain 6===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19491107}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19491107 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19491107}}

	==About this Structure==		==About this Structure==
	3FG7 is a 2 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=3FG7 OCA].		3FG7 is a 2 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=3FG7 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19491107</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burtnick, L D.]]		[[Category: Burtnick, L D.]]
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	[[Category: Villin head piece]]		[[Category: Villin head piece]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jul 8~~ 12~~:41~~:37 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 12 12:37:23 2009''