Fig. 3

Conservation and functional analysis of the p.V369 M mutation in USH2A. a Conservation of the Val369 residue of usherin protein. b Predicted secondary structures of the wild-type and mutant protein sequences flanking the mutations. The diagrams show the protein sequences with their secondary structures and their confidence values at the aligned positions. The secondary structure is annotated as follows: pink cylinder (alpha-helix); yellow arrow (beta-sheet); black line (coil); Conf, confidence; Pred, predict; H in Pred line (Helix); C in Pred line (coil); E in Pred line (sheet); AA, amino acid;, mutant amino acid. c Functional impact of the p.V369 M mutation on the partial tertiary structure of usherin protein by molecular modeling (PDB template: 4aqs.1.A; Identity 34.9%). The wild-type residue forms two salt bridges, with glutamic acid at position 367 and with phenylalanine at position 489, both of which were damaged by the mutant residues