View source for 3s90

==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=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3s90]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S90 FirstGlance]. <br>
</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='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>
</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_MOUSE 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. 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:21648001</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bricogne, G.]]
[[Category: Izard, T.]]
[[Category: Sharff, A.]]
[[Category: Yogesha, S D.]]
[[Category: Cell adhesion]]
[[Category: Focal adhesion]]
[[Category: Four-helix bundle]]