Fig. 2. BRAFV600E in complex with vemurafenib (cyan, PDB 3OG7) and PLX7904 (orange, PDB 4XV1). The surface of the N-methyl group of PLX7904 illustrates the reason for the Leu505 shift, which affects the conformation of the conserved RKTR motif (shown with sticks) at the dimer interface. Arg506 is particularly important for the stabilization of dimeric complexes. In the case of binding of a paradox-breaker, Arg506 in the αC-helix displays an outward movement which reduces the transactivation of ERK signalling. The protein surface of chains A and B is shown for 3OG7 only.
