6dv1
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the alpha-E-catenin actin-binding domain== | |
| + | <StructureSection load='6dv1' size='340' side='right' caption='[[6dv1]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6dv1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DV1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6dv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dv1 OCA], [http://pdbe.org/6dv1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dv1 RCSB], [http://www.ebi.ac.uk/pdbsum/6dv1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dv1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CTNA1_MOUSE CTNA1_MOUSE]] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.<ref>PMID:16325583</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | alpha-catenin is a key mechanosensor that forms force-dependent interactions with F-actin, thereby coupling the cadherin-catenin complex to the actin cytoskeleton at adherens junctions (AJs). However, the molecular mechanisms by which alpha-catenin engages F-actin under tension remained elusive. Here we show that the alpha1-helix of the alpha-catenin actin-binding domain (alphacat-ABD) is a mechanosensing motif that regulates tension-dependent F-actin binding and bundling. alphacat-ABD containing an alpha1-helix-unfolding mutation (H1) shows enhanced binding to F-actin in vitro. Although full-length alpha-catenin-H1 can generate epithelial monolayers that resist mechanical disruption, it fails to support normal AJ regulation in vivo. Structural and simulation analyses suggest that alpha1-helix allosterically controls the actin-binding residue V796 dynamics. Crystal structures of alphacat-ABD-H1 homodimer suggest that alpha-catenin can facilitate actin bundling while it remains bound to E-cadherin. We propose that force-dependent allosteric regulation of alphacat-ABD promotes dynamic interactions with F-actin involved in actin bundling, cadherin clustering, and AJ remodeling during tissue morphogenesis. | ||
| - | + | Force-dependent allostery of the alpha-catenin actin-binding domain controls adherens junction dynamics and functions.,Ishiyama N, Sarpal R, Wood MN, Barrick SK, Nishikawa T, Hayashi H, Kobb AB, Flozak AS, Yemelyanov A, Fernandez-Gonzalez R, Yonemura S, Leckband DE, Gottardi CJ, Tepass U, Ikura M Nat Commun. 2018 Nov 30;9(1):5121. doi: 10.1038/s41467-018-07481-7. PMID:30504777<ref>PMID:30504777</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 6dv1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ikura, M]] | [[Category: Ikura, M]] | ||
[[Category: Ishiyama, N]] | [[Category: Ishiyama, N]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: F-actin-binding]] | ||
| + | [[Category: Five-helix bundle]] | ||
| + | [[Category: Mechanosensor]] | ||
Revision as of 08:24, 19 December 2018
Crystal structure of the alpha-E-catenin actin-binding domain
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