Fig. 5.

Impact of PPARγ M280I and I290M mutations on the structure and dynamics. a Crystal structure of the PPARγ M280I LBD (plum) in complex with GW1929 (light red) and the PGC1α coactivator peptide (blue). The C-terminal H12 are shown in light pink. Right: Close-up of the regions around the mutation, showing its interactions stabilizing helix 3. b The atomic fluctuations calculated from the molecular dynamics simulation (last 10 ns) of the holo form of PPARγ complexes with rosiglitazone and coactivator peptide. The fluctuations are mapped onto the 3D surface of the proteins complexes. The color scale goes from blue (less flexible) to red (most flexible) between 0 and 2.5 Å. The thickness of the tube also reflects the flexibility (thicker corresponds to more flexible). Left: WT; middle: M280I; right: I290M