FIGURE 1.
Sequence alignment of the human PYDs. The six α helices of the PYDs with known structures are underlined and marked. The highly conserved residues (>80%) are shaded in yellow. The conserved lysine residue at the α2 helix is indicated with a magenta diamond. The acidic residues at the α1, α2, and α6 helices of the AIM2 PYD are shaded in red, the basic residues at the α5 and α6 helices are shaded in blue, the hydrophobic residues at the α2-α3 helices are shaded in green. Similarly, the acidic residues at the α1 and α4 helices and the basic residues at the α2 and α3 helices of the ASC PYD are shaded red and blue, respectively. Conserved residues among the PYHIN-only proteins are marked with orange boxes. The AIM2-specific residues within the PYHIN proteins are marked with black boxes.