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3jbi

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MDFF model of the vinculin tail domain bound to F-actin

3jbi, resolution 8.50Å

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 <SX load='3jbi' size='340' side='right' viewer='molstar' caption='[[3jbi]], [[Resolution|resolution]] 8.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3jbi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JBI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JBI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3jbi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] 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=3JBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JBI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 8.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jbj|3jbj]], [[3jbk|3jbk]]</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, VINC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=3jbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jbi OCA], [https://pdbe.org/3jbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jbi RCSB], [https://www.ebi.ac.uk/pdbsum/3jbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jbi ProSAT]</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=3jbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jbi OCA], [http://pdbe.org/3jbi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jbi RCSB], [http://www.ebi.ac.uk/pdbsum/3jbi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jbi ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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. [[http://www.uniprot.org/uniprot/VINC_CHICK VINC_CHICK]] 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:15229287</ref> <ref>PMID:20584916</ref> <ref>PMID:20086044</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;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3jbi" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Actin 3D structures|Actin 3D structures]]
 *[[Vinculin|Vinculin]]
-== References ==
-<references/>
 __TOC__
 </SX>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
 [[Category: Large Structures]]
 [[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: Adhesion]]
-[[Category: Cytoskeleton]]
-[[Category: Structural protein]]

3jbi

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MDFF model of the vinculin tail domain bound to F-actin

Structural highlights

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