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3s90

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Revision as of 18:27, 11 August 2016

Human vinculin head domain Vh1 (residues 1-252) in complex with murine talin (VBS33; residues 1512-1546)

Structural highlights

3s90 is a 4 chain structure with sequence from Human and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2x0c, 1syq, 1t01, 1rkc, 2bif, 3rf3
Gene:	VCL (HUMAN), Tln1, Tln (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[VINC_HUMAN] Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM: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.^[1] ^[2] Defects in VCL are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM: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.^[3]

Function

[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.^[4] [TLN1_MOUSE] 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.

Publication Abstract from PubMed

The cytoskeletal proteins talin and vinculin are localized at cell-matrix junctions and are key regulators of cell signaling, adhesion, and migration. Talin couples integrins via its FERM domain to F-actin and is an important regulator of integrin activation and clustering. The 220 kDa talin rod domain comprises several four- and five-helix bundles that harbor amphipathic alpha-helical vinculin binding sites (VBSs). In its inactive state the hydrophobic VBS residues involved in binding to vinculin are buried within these helix bundles, and mechanical force emanating from bound integrin receptors is thought necessary for their release and binding to vinculin. The crystal structure of a four-helix bundle of talin that harbors one of these VBSs, coined VBS33, was recently determined. Here we report the crystal structure of VBS33 in complex with vinculin at 2 A resolution. Notably, comparison of the native and vinculin bound structures shows that intermolecular interactions of the VBS33 alpha-helix with vinculin are more extensive than the intermolecular interactions of the VBS33 within the talin four-helix bundle.

Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin.,Yogesha SD, Sharff A, Bricogne G, Izard T Protein Sci. 2011 Jun 6. doi: 10.1002/pro.671. PMID:21648001^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Olson TM, Illenberger S, Kishimoto NY, Huttelmaier S, Keating MT, Jockusch BM. Metavinculin mutations alter actin interaction in dilated cardiomyopathy. Circulation. 2002 Jan 29;105(4):431-7. PMID:11815424
↑ Vasile VC, Will ML, Ommen SR, Edwards WD, Olson TM, Ackerman MJ. Identification of a metavinculin missense mutation, R975W, associated with both hypertrophic and dilated cardiomyopathy. Mol Genet Metab. 2006 Feb;87(2):169-74. Epub 2005 Oct 19. PMID:16236538 doi:S1096-7192(05)00258-1
↑ Vasile VC, Ommen SR, Edwards WD, Ackerman MJ. A missense mutation in a ubiquitously expressed protein, vinculin, confers susceptibility to hypertrophic cardiomyopathy. Biochem Biophys Res Commun. 2006 Jul 7;345(3):998-1003. Epub 2006 May 4. PMID:16712796 doi:S0006-291X(06)00981-8
↑ Le Clainche C, Dwivedi SP, Didry D, Carlier MF. Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein. J Biol Chem. 2010 Jul 23;285(30):23420-32. doi: 10.1074/jbc.M110.102830. Epub, 2010 May 18. PMID:20484056 doi:10.1074/jbc.M110.102830
↑ Yogesha SD, Sharff A, Bricogne G, Izard T. Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin. Protein Sci. 2011 Jun 6. doi: 10.1002/pro.671. PMID:21648001 doi:10.1002/pro.671

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3s90"

@@ Line 1: / Line 1: @@
 ==Human vinculin head domain Vh1 (residues 1-252) in complex with murine talin (VBS33; residues 1512-1546)==
 <StructureSection load='3s90' size='340' side='right' caption='[[3s90]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x0c|2x0c]], [[1syq|1syq]], [[1t01|1t01]], [[1rkc|1rkc]], [[2bif|2bif]], [[3rf3|3rf3]]</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, Tln ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3s90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s90 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s90 RCSB], [http://www.ebi.ac.uk/pdbsum/3s90 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=3s90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s90 OCA], [http://pdbe.org/3s90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s90 RCSB], [http://www.ebi.ac.uk/pdbsum/3s90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3s90 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3s90" style="background-color:#fffaf0;"></div>
 ==See Also==

3s90

From Proteopedia

Revision as of 18:27, 11 August 2016

Human vinculin head domain Vh1 (residues 1-252) in complex with murine talin (VBS33; residues 1512-1546)

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

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