3jbj

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3jbj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JBJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3jbj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JBJ FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3jbi|3jbi]], [[3jbk|3jbk]]</div></td></tr>
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<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jbj OCA], [https://pdbe.org/3jbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jbj RCSB], [https://www.ebi.ac.uk/pdbsum/3jbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jbj 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=3jbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jbj OCA], [https://pdbe.org/3jbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jbj RCSB], [https://www.ebi.ac.uk/pdbsum/3jbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jbj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3jbj" 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]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Alushin, G M]]
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[[Category: Alushin GM]]
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[[Category: Campbell, S L]]
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[[Category: Campbell SL]]
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[[Category: Kim, L Y]]
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[[Category: Kim LY]]
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[[Category: Lee, H T]]
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[[Category: Lee HT]]
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[[Category: Pershad, M]]
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[[Category: Pershad M]]
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[[Category: Thompson, P M]]
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[[Category: Thompson PM]]
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[[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: Structural protein]]
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Current revision

Cryo-EM reconstruction of F-actin

3jbj, resolution 7.60Å

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