1yri - Revision history

OCA at 07:00, 23 August 2023

OCA — Wed, 23 Aug 2023 07:00:32 GMT

←Older revision		Revision as of 07:00, 23 August 2023
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	<StructureSection load='1yri' size='340' side='right'caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>		<StructureSection load='1yri' size='340' side='right'caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YRI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YRI FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>~~, ~~<scene name='pdbligand=IOD:IODIDE+ION'>IOD</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]] 1Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1yrf\|1yrf]]~~, ~~[[1wy3\|1wy3]], [[1wy4\|1wy4]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [https://pdbe.org/1yri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [https://www.ebi.ac.uk/pdbsum/1yri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yri 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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [https://pdbe.org/1yri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [https://www.ebi.ac.uk/pdbsum/1yri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yri ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/VILI_CHICK VILI_CHICK]] 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 (By similarity). Its actin-bundling activity is inhibited by tropomyosin.<ref>PMID:3793760</ref> <ref>PMID:1618806</ref>	+	[https://www.uniprot.org/uniprot/VILI_CHICK VILI_CHICK] 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 (By similarity). Its actin-bundling activity is inhibited by tropomyosin.<ref>PMID:3793760</ref> <ref>PMID:1618806</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: Gallus gallus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chiu~~, T K~~]]	+	[[Category: Chiu TK]]
-	[[Category: Davies~~, D R~~]]	+	[[Category: Davies DR]]
-	[[Category: Eaton~~, W A~~]]	+	[[Category: Eaton WA]]
-	[[Category: Herbst-Irmer, R]]	+	[[Category: Herbst-Irmer R]]
-	[[Category: Hofrichter, J]]	+	[[Category: Hofrichter J]]
-	[[Category: Kubelka, J]]	+	[[Category: Kubelka J]]
-	~~[[Category: Structural protein]]~~	+
-	~~[[Category: Villin headpiece subdomain~~]]	+

OCA at 09:08, 21 April 2021

OCA — Wed, 21 Apr 2021 09:08:37 GMT

←Older revision		Revision as of 09:08, 21 April 2021
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	<StructureSection load='1yri' size='340' side='right'caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>		<StructureSection load='1yri' size='340' side='right'caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1YRI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YRI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</div></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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [~~http~~://pdbe.org/1yri PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1yri PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1yri 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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [https://pdbe.org/1yri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [https://www.ebi.ac.uk/pdbsum/1yri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yri ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/VILI_CHICK VILI_CHICK]] 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 (By similarity). Its actin-bundling activity is inhibited by tropomyosin.<ref>PMID:3793760</ref> <ref>PMID:1618806</ref>	+	[[https://www.uniprot.org/uniprot/VILI_CHICK VILI_CHICK]] 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 (By similarity). Its actin-bundling activity is inhibited by tropomyosin.<ref>PMID:3793760</ref> <ref>PMID:1618806</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:29, 17 July 2019

OCA — Wed, 17 Jul 2019 13:29:08 GMT

←Older revision		Revision as of 13:29, 17 July 2019
Line 1:		Line 1:

	==Chicken villin subdomain HP-35, N68H, pH6.4==		==Chicken villin subdomain HP-35, N68H, pH6.4==
-	<StructureSection load='1yri' size='340' side='right' caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>	+	<StructureSection load='1yri' size='340' side='right'caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YRI FirstGlance]. <br>		<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YRI FirstGlance]. <br>
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/yr/1yri_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yr/1yri_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 1yri" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1yri" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Villin\|Villin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Chiu, T K]]		[[Category: Chiu, T K]]
	[[Category: Davies, D R]]		[[Category: Davies, D R]]

OCA at 09:23, 12 October 2017

OCA — Thu, 12 Oct 2017 09:23:06 GMT

←Older revision		Revision as of 09:23, 12 October 2017
Line 1:		Line 1:
		+
	==Chicken villin subdomain HP-35, N68H, pH6.4==		==Chicken villin subdomain HP-35, N68H, pH6.4==
	<StructureSection load='1yri' size='340' side='right' caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>		<StructureSection load='1yri' size='340' side='right' caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [http://pdbe.org/1yri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [http://www.ebi.ac.uk/pdbsum/1yri 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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [http://pdbe.org/1yri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [http://www.ebi.ac.uk/pdbsum/1yri PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yri ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1yri" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1yri" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Villin\|Villin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:18, 7 February 2016

OCA — Sun, 07 Feb 2016 19:18:47 GMT

←Older revision		Revision as of 19:18, 7 February 2016
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	<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=1yri ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:19, 10 September 2015

OCA — Thu, 10 Sep 2015 04:19:03 GMT

←Older revision		Revision as of 04:19, 10 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [http://www.ebi.ac.uk/pdbsum/1yri 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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [http://pdbe.org/1yri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [http://www.ebi.ac.uk/pdbsum/1yri PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1yri" style="background-color:#fffaf0;"></div>

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

OCA at 17:40, 24 December 2014

OCA — Wed, 24 Dec 2014 17:40:41 GMT

←Older revision		Revision as of 17:40, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YRI FirstGlance]. <br>		<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YRI FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [http://www.ebi.ac.uk/pdbsum/1yri 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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [http://www.ebi.ac.uk/pdbsum/1yri PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VILI_CHICK VILI_CHICK]] 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 (By similarity). Its actin-bundling activity is inhibited by tropomyosin.<ref>PMID:3793760</ref> <ref>PMID:1618806</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Chiu, T K.]]	+	[[Category: Chiu, T K]]
-	[[Category: Davies, D R.]]	+	[[Category: Davies, D R]]
-	[[Category: Eaton, W A.]]	+	[[Category: Eaton, W A]]
-	[[Category: Herbst-Irmer, R.]]	+	[[Category: Herbst-Irmer, R]]
-	[[Category: Hofrichter, J.]]	+	[[Category: Hofrichter, J]]
-	[[Category: Kubelka, J.]]	+	[[Category: Kubelka, J]]
	[[Category: Structural protein]]		[[Category: Structural protein]]
	[[Category: Villin headpiece subdomain]]		[[Category: Villin headpiece subdomain]]

OCA at 19:45, 28 September 2014

OCA — Sun, 28 Sep 2014 19:45:54 GMT

←Older revision		Revision as of 19:45, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1yri.~~png~~\|~~left~~\|200px]]	+	==Chicken villin subdomain HP-35, N68H, pH6.4==
		+	<StructureSection load='1yri' size='340' side='right' caption='[[1yri]], [[Resolution\|resolution]] 1.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YRI FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yrf\|1yrf]], [[1wy3\|1wy3]], [[1wy4\|1wy4]]</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=1yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yri OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yri RCSB], [http://www.ebi.ac.uk/pdbsum/1yri 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/yr/1yri_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 35-residue subdomain of the villin headpiece (HP35) is a small ultrafast folding protein that is being intensely studied by experiments, theory, and simulations. We have solved the x-ray structures of HP35 and its fastest folding mutant [K24 norleucine (nL)] to atomic resolution and compared their experimentally measured folding kinetics by using laser temperature jump. The structures, which are in different space groups, are almost identical to each other but differ significantly from previously solved NMR structures. Hence, the differences between the x-ray and NMR structures are probably not caused by lattice contacts or crystal/solution differences, but reflect the higher accuracy of the x-ray structures. The x-ray structures reveal important details of packing of the hydrophobic core and some additional features, such as cross-helical H bonds. Comparison of the x-ray structures indicates that the nL substitution produces only local perturbations. Consequently, the finding that the small stabilization by the mutation is completely reflected in an increased folding rate suggests that this region of the protein is as structured in the transition state as in the folded structure. It is therefore a target for engineering to increase the folding rate of the subdomain from approximately 0.5 micros(-1) for the nL mutant to the estimated theoretical speed limit of approximately 3 micros(-1).

-	~~{{STRUCTURE_1yri\| PDB=1yri \| SCENE= }}~~	+	High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.,Chiu TK, Kubelka J, Herbst-Irmer R, Eaton WA, Hofrichter J, Davies DR Proc Natl Acad Sci U S A. 2005 May 24;102(21):7517-22. Epub 2005 May 13. PMID:15894611<ref>PMID:15894611</ref>

-	~~===Chicken villin subdomain HP-35~~, ~~N68H, pH6.4===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15894611}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1yri]] is~~ a ~~1 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=1YRI OCA].~~	+

	==See Also==		==See Also==
	*[[Villin\|Villin]]		*[[Villin\|Villin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:015894611<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Chiu, T K.]]		[[Category: Chiu, T K.]]
	[[Category: Davies, D R.]]		[[Category: Davies, D R.]]

OCA at 07:37, 20 October 2012

OCA — Sat, 20 Oct 2012 07:37:05 GMT

←Older revision		Revision as of 07:37, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1yri]] is a 1 chain structure ~~of [[Villin]]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA].	+	[[1yri]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRI OCA].

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

OCA at 16:54, 25 July 2012

OCA — Wed, 25 Jul 2012 16:54:00 GMT

←Older revision		Revision as of 16:54, 25 July 2012
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	[[Image:1yri.png\|left\|200px]]		[[Image:1yri.png\|left\|200px]]

-	<!--
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-	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),
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	{{STRUCTURE_1yri\| PDB=1yri \| SCENE= }}		{{STRUCTURE_1yri\| PDB=1yri \| SCENE= }}

	===Chicken villin subdomain HP-35, N68H, pH6.4===		===Chicken villin subdomain HP-35, N68H, pH6.4===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15894611}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15894611 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_15894611}}		{{ABSTRACT_PUBMED_15894611}}

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	==See Also==		==See Also==
-	*[[Villin]]	+	*[[Villin\|Villin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15894611~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015894611</ref><references group="xtra"/>
	[[Category: Chiu, T K.]]		[[Category: Chiu, T K.]]
	[[Category: Davies, D R.]]		[[Category: Davies, D R.]]