Figure 2 Bioinformatic studies of MORC2 mutations
A. MORC2 protein (NP_001290185) predicted domains. An N-terminal GHJL-type ATPase domain together with a ribosomal protein S5 (RPS5; OMIM 603630) form the functional ATPase catalytic site. CC: coiled-coil regions required for protein dimerization. CW: a zinc finger-type CW domain allowing interaction with DNA. CD: a chromo-like domain recognizing methylated histone proteins. B. Multiple alignments of MORC2 orthologous genes selected from 401 to 480 amino acids in MORC2 human protein. Black arrows indicate known mutation in the area. Red arrows indicate mutation positions in patients families 1 and 2 describes here. Colour amino acids follow RasMol color scheme according to traditional amino acid properties. Outer parts of a protein that are polar are visible (bright) colors and non-polar residues darker. Conservation level is indicated by a bar plot. C. Three-dimensional structure of homodimeric human MORC2 focused on S5 transactivator domain showing the localization of mutated residue (light green) on chain A (dark green).