4dj9 - Revision history

OCA at 10:48, 1 March 2024

OCA — Fri, 01 Mar 2024 10:48:51 GMT

←Older revision		Revision as of 10:48, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dj9]] 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=4DJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DJ9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dj9]] 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=4DJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DJ9 FirstGlance]. <br>
-	</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=4dj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dj9 OCA], [https://pdbe.org/4dj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dj9 RCSB], [https://www.ebi.ac.uk/pdbsum/4dj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dj9 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.25Å</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=4dj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dj9 OCA], [https://pdbe.org/4dj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dj9 RCSB], [https://www.ebi.ac.uk/pdbsum/4dj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dj9 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:[https://omim.org/entry/611407 611407]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11815424</ref> <ref>PMID:16236538</ref> Defects in VCL are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM:[https://omim.org/entry/613255 613255]]. It is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:16712796</ref>	+	[https://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN] Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:[https://omim.org/entry/611407 611407]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11815424</ref> <ref>PMID:16236538</ref> Defects in VCL are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM:[https://omim.org/entry/613255 613255]. It is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:16712796</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:20484056</ref>	+	[https://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:20484056</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The cytoskeletal protein talin activates integrin receptors by binding of its FERM domain to the cytoplasmic tail of beta-integrin. Talin also couples integrins to the actin cytoskeleton, largely by binding to and activating the cytoskeletal protein vinculin, which binds to F-actin through the agency of its five-helix bundle tail (Vt) domain. Talin activates vinculin by means of buried amphipathic alpha-helices coined vinculin binding sites (VBSs) that reside within numerous four- and five-helix bundle domains that comprise the central talin rod, which are released from their buried locales by means of mechanical tension on the integrin:talin complex. In turn, these VBSs bind to the N-terminal seven-helix bundle (Vh1) domain of vinculin, creating an entirely new helix bundle that severs its head-tail interactions. Interestingly, talin harbors a second integrin binding site coined IBS2 that consists of two five-helix bundle domains that also contain a VBS (VBS50). Here we report the crystal structure of VBS50 in complex with vinculin at 2.3 A resolution and show that intramolecular interactions of VBS50 within IBS2 are much more extensive versus its interactions with vinculin. Indeed, the IBS2-vinculin interaction only occurs at physiological temperature and the affinity of VBS50 for vinculin is about 30 times less than other VBSs. The data support a model where integrin binding destabilizes IBS2 to allow it to bind to vinculin.	+
-		+
-	Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin.,Yogesha SD, Rangarajan ES, Vonrhein C, Bricogne G, Izard T Protein Sci. 2012 Feb 14. doi: 10.1002/pro.2041. PMID:22334306<ref>PMID:22334306</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4dj9" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
-	*[[Talin\|Talin]]	+	*[[Talin 3D structures\|Talin 3D structures]]
	*[[Vinculin\|Vinculin]]		*[[Vinculin\|Vinculin]]
	== References ==		== References ==

OCA at 08:21, 21 September 2022

OCA — Wed, 21 Sep 2022 08:21:06 GMT

←Older revision		Revision as of 08:21, 21 September 2022
Line 1:		Line 1:

	==Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)==		==Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)==
-	<StructureSection load='4dj9' size='340' side='right' caption='[[4dj9]], [[Resolution\|resolution]] 2.25Å' scene=''>	+	<StructureSection load='4dj9' size='340' side='right'caption='[[4dj9]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dj9]] 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=4DJ9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DJ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dj9]] 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=4DJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DJ9 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rkc\|1rkc]], [[1syq\|1syq]], [[3s90\|3s90]], [[3tj5\|3tj5]], [[3tj6\|3tj6]], [[1rke\|1rke]]</td></tr>	+	</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=4dj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dj9 OCA], [https://pdbe.org/4dj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dj9 RCSB], [https://www.ebi.ac.uk/pdbsum/4dj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dj9 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TLN1, KIAA1027, TLN ([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=4dj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dj9 OCA], [~~http~~://pdbe.org/4dj9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4dj9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4dj9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4dj9 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:[~~http~~://omim.org/entry/611407 611407]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11815424</ref> <ref>PMID:16236538</ref> Defects in VCL are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM:[~~http~~://omim.org/entry/613255 613255]]. It is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:16712796</ref>	+	[[https://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:[https://omim.org/entry/611407 611407]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11815424</ref> <ref>PMID:16236538</ref> Defects in VCL are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM:[https://omim.org/entry/613255 613255]]. It is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:16712796</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:20484056</ref> [[http://www.uniprot.org/uniprot/TLN1_HUMAN TLN1_HUMAN]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity).	+	[[https://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:20484056</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Bricogne, G]]	+	[[Category: Large Structures]]
-	[[Category: Izard, T]]	+	[[Category: Bricogne G]]
-	[[Category: Rangarajan~~, E S~~]]	+	[[Category: Izard T]]
-	[[Category: Vonrhein, C]]	+	[[Category: Rangarajan ES]]
-	[[Category: Yogesha~~, S D]]~~	+	[[Category: Vonrhein C]]
-	~~[[Category: Cell adhesion]]~~	+	[[Category: Yogesha SD]]
-	~~[[Category: Cytoskeleton]]~~	+
-	~~[[Category: Cytosol]]~~	+
-	~~[[Category: F-actin]]~~	+
-	~~[[Category: Focal adhesion]]~~	+
-	~~[[Category: Four-helix bundle]]~~	+
-	~~[[Category: Protein-protein interaction~~]]	+

OCA at 07:57, 5 August 2016

OCA — Fri, 05 Aug 2016 07:57:39 GMT

←Older revision		Revision as of 07:57, 5 August 2016
Line 1:		Line 1:
		+
	==Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)==		==Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)==
	<StructureSection load='4dj9' size='340' side='right' caption='[[4dj9]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='4dj9' size='340' side='right' caption='[[4dj9]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dj9]] 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=4DJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DJ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dj9]] 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=4DJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DJ9 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rkc\|1rkc]], [[1syq\|1syq]], [[3s90\|3s90]], [[3tj5\|3tj5]], [[3tj6\|3tj6]], [[1rke\|1rke]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rkc\|1rkc]], [[1syq\|1syq]], [[3s90\|3s90]], [[3tj5\|3tj5]], [[3tj6\|3tj6]], [[1rke\|1rke]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), TLN1, KIAA1027, TLN ([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">VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TLN1, KIAA1027, TLN ([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=4dj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dj9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dj9 RCSB], [http://www.ebi.ac.uk/pdbsum/4dj9 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=4dj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dj9 OCA], [http://pdbe.org/4dj9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dj9 RCSB], [http://www.ebi.ac.uk/pdbsum/4dj9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dj9 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	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 4dj9" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Bricogne, G]]		[[Category: Bricogne, G]]
	[[Category: Izard, T]]		[[Category: Izard, T]]

OCA at 08:45, 21 December 2014

OCA — Sun, 21 Dec 2014 08:45:11 GMT

←Older revision		Revision as of 08:45, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4dj9\| PDB=4dj9 \| SCENE= }}~~	+	==Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)==
-	===Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)===	+	<StructureSection load='4dj9' size='340' side='right' caption='[[4dj9]], [[Resolution\|resolution]] 2.25Å' scene=''>
-	~~{{ABSTRACT_PUBMED_22334306}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4dj9]] 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=4DJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DJ9 FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rkc\|1rkc]], [[1syq\|1syq]], [[3s90\|3s90]], [[3tj5\|3tj5]], [[3tj6\|3tj6]], [[1rke\|1rke]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), TLN1, KIAA1027, TLN ([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=4dj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dj9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dj9 RCSB], [http://www.ebi.ac.uk/pdbsum/4dj9 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:[http://omim.org/entry/611407 611407]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11815424</ref> <ref>PMID:16236538</ref> Defects in VCL are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM:[http://omim.org/entry/613255 613255]]. It is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:16712796</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:20484056</ref> [[http://www.uniprot.org/uniprot/TLN1_HUMAN TLN1_HUMAN]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The cytoskeletal protein talin activates integrin receptors by binding of its FERM domain to the cytoplasmic tail of beta-integrin. Talin also couples integrins to the actin cytoskeleton, largely by binding to and activating the cytoskeletal protein vinculin, which binds to F-actin through the agency of its five-helix bundle tail (Vt) domain. Talin activates vinculin by means of buried amphipathic alpha-helices coined vinculin binding sites (VBSs) that reside within numerous four- and five-helix bundle domains that comprise the central talin rod, which are released from their buried locales by means of mechanical tension on the integrin:talin complex. In turn, these VBSs bind to the N-terminal seven-helix bundle (Vh1) domain of vinculin, creating an entirely new helix bundle that severs its head-tail interactions. Interestingly, talin harbors a second integrin binding site coined IBS2 that consists of two five-helix bundle domains that also contain a VBS (VBS50). Here we report the crystal structure of VBS50 in complex with vinculin at 2.3 A resolution and show that intramolecular interactions of VBS50 within IBS2 are much more extensive versus its interactions with vinculin. Indeed, the IBS2-vinculin interaction only occurs at physiological temperature and the affinity of VBS50 for vinculin is about 30 times less than other VBSs. The data support a model where integrin binding destabilizes IBS2 to allow it to bind to vinculin.

-	~~==Disease==~~	+	Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin.,Yogesha SD, Rangarajan ES, Vonrhein C, Bricogne G, Izard T Protein Sci. 2012 Feb 14. doi: 10.1002/pro.2041. PMID:22334306<ref>PMID:22334306</ref>
-	~~[[http://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Defects~~ in ~~VCL are the cause of cardiomyopathy dilated type 1W~~ (~~CMD1W~~) ~~[MIM:[http://omim.org/entry/611407 611407]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function~~, ~~resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11815424</ref><ref>PMID:16236538</ref> Defects in VCL are~~ the ~~cause of familial hypertrophic cardiomyopathy type 15~~ (~~CMH15~~) ~~[MIM:[http://omim~~.~~org/entry/613255 613255]]. It is a hereditary heart disorder characterized by ventricular hypertrophy~~, ~~which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea~~, ~~syncope~~, ~~collapse~~, ~~palpitations~~, ~~and chest pain~~. ~~They can be readily provoked by exercise~~. ~~The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death~~.<ref>PMID:~~16712796~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.org/uniprot/VINC_HUMAN VINC_HUMAN]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<~~ref~~>~~PMID:20484056~~</~~ref~~> [[http://www.uniprot.org/uniprot/TLN1_HUMAN TLN1_HUMAN]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity).	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[4dj9]] 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=4DJ9 OCA].	+

	==See Also==		==See Also==
	*[[Talin\|Talin]]		*[[Talin\|Talin]]
	*[[Vinculin\|Vinculin]]		*[[Vinculin\|Vinculin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:022334306</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Bricogne, G.]]	+	[[Category: Bricogne, G]]
-	[[Category: Izard, T.]]	+	[[Category: Izard, T]]
-	[[Category: Rangarajan, E S.]]	+	[[Category: Rangarajan, E S]]
-	[[Category: Vonrhein, C.]]	+	[[Category: Vonrhein, C]]
-	[[Category: Yogesha, S D.]]	+	[[Category: Yogesha, S D]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]
	[[Category: Cytoskeleton]]		[[Category: Cytoskeleton]]

OCA at 18:09, 24 March 2013

OCA — Sun, 24 Mar 2013 18:09:09 GMT

←Older revision		Revision as of 18:09, 24 March 2013
Line 1:		Line 1:
-	[[Image:4dj9.png\|left\|200px]]
-
	{{STRUCTURE_4dj9\| PDB=4dj9 \| SCENE= }}		{{STRUCTURE_4dj9\| PDB=4dj9 \| SCENE= }}
-
	===Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)===		===Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)===
		+	{{ABSTRACT_PUBMED_22334306}}

-	~~{{ABSTRACT_PUBMED_22334306}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:[http://omim.org/entry/611407 611407]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11815424</ref><ref>PMID:16236538</ref> Defects in VCL are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM:[http://omim.org/entry/613255 613255]]. It is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:16712796</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:20484056</ref> [[http://www.uniprot.org/uniprot/TLN1_HUMAN TLN1_HUMAN]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity).

	==About this Structure==		==About this Structure==
Line 15:		Line 17:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:022334306</ref><references group="xtra"/>	+	<ref group="xtra">PMID:022334306</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bricogne, G.]]		[[Category: Bricogne, G.]]

OCA at 10:41, 20 October 2012

OCA — Sat, 20 Oct 2012 10:41:05 GMT

←Older revision		Revision as of 10:41, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[4dj9]] is a 2 chain structure ~~of [[Talin]] and [[Vinculin]]~~ 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=4DJ9 OCA].	+	[[4dj9]] 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=4DJ9 OCA].

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

OCA at 02:56, 26 July 2012

OCA — Thu, 26 Jul 2012 02:56:03 GMT

←Older revision		Revision as of 02:56, 26 July 2012
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	[[Image:4dj9.png\|left\|200px]]		[[Image:4dj9.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_4dj9", 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_4dj9\| PDB=4dj9 \| SCENE= }}		{{STRUCTURE_4dj9\| PDB=4dj9 \| SCENE= }}

	===Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)===		===Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_22334306}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 22334306 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_22334306}}		{{ABSTRACT_PUBMED_22334306}}

	==About this Structure==		==About this Structure==
-	[[4dj9]] 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=4DJ9 OCA].	+	[[4dj9]] is a 2 chain structure of [[Talin]] and [[Vinculin]] 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=4DJ9 OCA].
		+
		+	==See Also==
		+	*[[Talin\|Talin]]
		+	*[[Vinculin\|Vinculin]]

	==Reference==		==Reference==

OCA at 08:22, 16 May 2012

OCA — Wed, 16 May 2012 08:22:57 GMT

←Older revision		Revision as of 08:22, 16 May 2012
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-	[[Image:4dj9.~~jpg~~\|left\|200px]]	+	[[Image:4dj9.png\|left\|200px]]

	<!--		<!--

OCA at 08:44, 29 February 2012

OCA — Wed, 29 Feb 2012 08:44:07 GMT

←Older revision		Revision as of 08:44, 29 February 2012
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-	~~'''Unreleased structure'''~~	+	[[Image:4dj9.jpg\|left\|200px]]

-	The ~~entry 4dj9~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_4dj9", 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_4dj9\| PDB=4dj9 \| SCENE= }}

-	~~Authors: Yogesha~~, ~~S.D., Rangarajan, E.S., Vonrhein, C., Bricogne, G., Izard, T.~~	+	===Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)===

-	~~Description: Human vinculin head domain Vh1 (residues 1~~-~~258) in complex with~~ the ~~talin vinculin binding site 50~~ (~~VBS50~~, ~~residues 2078~~-~~2099)~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22334306}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22334306 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22334306}}
		+
		+	==About this Structure==
		+	[[4dj9]] 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=4DJ9 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022334306</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Bricogne, G.]]
		+	[[Category: Izard, T.]]
		+	[[Category: Rangarajan, E S.]]
		+	[[Category: Vonrhein, C.]]
		+	[[Category: Yogesha, S D.]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Cytoskeleton]]
		+	[[Category: Cytosol]]
		+	[[Category: F-actin]]
		+	[[Category: Focal adhesion]]
		+	[[Category: Four-helix bundle]]
		+	[[Category: Protein-protein interaction]]

OCA: Protected "4dj9" [edit=sysop:move=sysop]

OCA — Wed, 08 Feb 2012 06:14:02 GMT

Protected "4dj9" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:14, 8 February 2012