6duw | pdb_00006duw

Crystal structure of the alpha-N-catenin actin-binding domain H1 mutant

spinqualitylabelsall models 6duw, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6duw is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CTNNA2, CAPR (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catenin 3D structures

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