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| <SX load='3jbk' size='340' side='right' viewer='molstar' caption='[[3jbk]], [[Resolution|resolution]] 8.20Å' scene=''> | | <SX load='3jbk' size='340' side='right' viewer='molstar' caption='[[3jbk]], [[Resolution|resolution]] 8.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3jbk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JBK FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3jbk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JBK FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.2Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3jbi|3jbi]], [[3jbj|3jbj]]</div></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VCL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jbk OCA], [https://pdbe.org/3jbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jbk RCSB], [https://www.ebi.ac.uk/pdbsum/3jbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jbk 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=3jbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jbk OCA], [https://pdbe.org/3jbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jbk RCSB], [https://www.ebi.ac.uk/pdbsum/3jbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jbk ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease ==
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| [[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>
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| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[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/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Vinculin is an essential adhesion protein that links membrane-bound integrin and cadherin receptors through their intracellular binding partners to filamentous actin, facilitating mechanotransduction. Here we present an 8.5-A-resolution cryo-electron microscopy reconstruction and pseudo-atomic model of the vinculin tail (Vt) domain bound to F-actin. Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the Vt helical bundle to mediate actin bundling. We find that an analogous conformational change also occurs in the H1' helix of the tail domain of metavinculin (MVt) upon actin binding, a muscle-specific splice isoform that suppresses actin bundling by Vt. These data support a model in which metavinculin tunes the actin bundling activity of vinculin in a tissue-specific manner, providing a mechanistic framework for understanding metavinculin mutations associated with hereditary cardiomyopathies.
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| The Structural Basis of Actin Organization by Vinculin and Metavinculin.,Kim LY, Thompson PM, Lee HT, Pershad M, Campbell SL, Alushin GM J Mol Biol. 2016 Jan 16;428(1):10-25. doi: 10.1016/j.jmb.2015.09.031. Epub 2015, Oct 20. PMID:26493222<ref>PMID:26493222</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3jbk" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Actin 3D structures|Actin 3D structures]] | | *[[Actin 3D structures|Actin 3D structures]] |
| *[[Vinculin|Vinculin]] | | *[[Vinculin|Vinculin]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| [[Category: Alushin, G M]] | | [[Category: Alushin GM]] |
| [[Category: Campbell, S L]] | | [[Category: Campbell SL]] |
| [[Category: Kim, L Y]] | | [[Category: Kim LY]] |
| [[Category: Lee, H T]] | | [[Category: Lee HT]] |
| [[Category: Pershad, M]] | | [[Category: Pershad M]] |
| [[Category: Thompson, P M]] | | [[Category: Thompson PM]] |
| [[Category: Actin]]
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| [[Category: Adhesion]]
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| [[Category: Cell migration]]
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| [[Category: Cytoskeleton]]
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| [[Category: Mechanosensation]]
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| [[Category: Metavinculin]]
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| [[Category: Structural protein]]
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| [[Category: Vinculin]]
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