FIGURE 2.

PHF6 extended PHD2 domain is composed of a pre-PHD zinc finger and a noncanonical PHD finger. A, schematic representation of the functional domains and locations of mutations in the human PHF6 protein. Four nuclear localization signals are shown in yellow. Filled triangles represent PHF6 mutations found in BFLS patients. PHF6 mutations identified in acute myeloid leukemia patients are depicted as open circles. Mutations in T-ALL samples are shown above the box. B, secondary structural elements in the PHF6-ePHD2 domain. The N-terminal pre-PHD zinc finger is indicated by a green bar, the PHD finger by a sky blue bar, and the middle region by a magenta bar. The conserved zinc-chelating residues are marked as orange vertical bars. Residues that are involved in zinc ions coordination are connected by solid lines (the first, second, and third tetrads are connected by gray, purple, and orange lines, respectively). C, schematic representation of the PHF6-ePHD2 domain highlights the secondary structural elements, color scheme as for B, and spheres are zinc ions. D, schematic showing the zinc-binding topology and secondary structural elements of the ePHD2 domain, color scheme as for B. β-Strands are labeled β1–β6 and helices α1–α5. Cys and His residues are shown as circles and squares. E, surface view of the ePHD2 domain structure shown in C (right), color scheme as for B.