Figure 2. Modeling of the effects of the Arg343Trp mutation on TP63 structure. Beginning from a TP63 crystal structure, mutation of residue 343 from Arg to Trp followed by side-chain repacking demonstrates a loss of favorable electrostatic contacts between wild-type Arg and negatively charged phosphates of the accompanying double stranded DNA. This suggests that the functional consequence of Trp is diminished binding affinity and thereby a change (i.e., a reduction) in transcriptional control. The wild-type structure of TP63 (with an Arg residue at position 343) is shown in blue, the mutant structure with a Trp residue at position 343 is shown in yellow, and a DNA helix is shown in brown and green.