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).