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| | <StructureSection load='6duw' size='340' side='right'caption='[[6duw]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='6duw' size='340' side='right'caption='[[6duw]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6duw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DUW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DUW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6duw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DUW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTNNA2, CAPR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=6duw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6duw OCA], [http://pdbe.org/6duw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6duw RCSB], [http://www.ebi.ac.uk/pdbsum/6duw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6duw 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=6duw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6duw OCA], [https://pdbe.org/6duw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6duw RCSB], [https://www.ebi.ac.uk/pdbsum/6duw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6duw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CTNA2_HUMAN CTNA2_HUMAN]] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.[UniProtKB:Q61301] | + | [https://www.uniprot.org/uniprot/CTNA2_HUMAN CTNA2_HUMAN] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.[UniProtKB:Q61301] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[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]]
| + | |
| Structural highlights
Function
CTNA2_HUMAN May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.[UniProtKB:Q61301]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Force-dependent allostery of the alpha-catenin actin-binding domain controls adherens junction dynamics and functions. Nat Commun. 2018 Nov 30;9(1):5121. doi: 10.1038/s41467-018-07481-7. PMID:30504777 doi:http://dx.doi.org/10.1038/s41467-018-07481-7
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