Fig. 2

Conservation and functional analysis of the p.R161C mutation in DCHS1. a Conservation of the Arg161 residue of protocadherin-16. 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, predictrf; 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.R161C mutation on the partial tertiary structure of protocadherin-16 protein predicted by molecular modeling (PDB template: 5szn.1.A; Identity 39.3%). The wild-type residue forms a salt bridge with the glutamic acid residue at position 206, with this binding damaged by substitution of the mutant residue