Fig. 5
Identification of the critical actin-binding site residues in α-catenin. a Model of the αcat-ABD (red) bound to two axially adjacent actin monomers (dark and light teal) within F-actin, based on the vin-ABD/F-actin cryo-EM structure (PDB ID: 3JBI). b Comparison of high-resolution crystal structures of αEcat-ABD-WT (red) and αNcat-ABD-WT (blue). The overall structure of αEcat-ABD-WT closely resembles αNcat-ABD-WT, as two ABD structures can be superposed with RMSD of 0.53 Å over 156 residues. A close-up view (right) shows that αEcat-ABD-WT contains a cavity (pink molecular envelope), which could accommodate V796 in a cryptic state similar to V796N in the αNcat-ABD-WT structure. c Actin cosedimentation assays of αEcat-ABD variants: WT, L785A, I792A, V796A, 3A, V714A, H1, H1L785A, H1I792A, and H1V796A. Data are presented as mean ± SEM (N = 3). Significance by ANOVA: **P < 0.01, ***P < 0.001
