Figure 1

In silico analysis and molecular modeling of the wild-type and mutant POU3F4 proteins. The p.Glu236Ala (p.E236A) mutation possibly interferes with the stability between the secondary structures of the protein (A). The p.Pro301Leu (p.P301L) mutation affects the structure of the turn and the turn becomes shorter (B). The hydroxide group introduced by the p.Ile308Thr (p.I308T) mutation causes a conformational change in the Arginine residue at 323 (C). Schematic illustration of POU3F4 protein labeled with the five mutations identified in this study (D).