Fig. 4
From: Recurrent activating mutations of PPARγ associated with luminal bladder tumors
Structural properties of PPARγ T475M. a Crystal structure of the PPARγ T475M LBD (red) in complex with GW1929 (violet) and the PGC1α coactivator peptide (blue). The C-terminal H12 helices are shown in light pink. Overall fold of the homodimer complex, showing the T475M mutations at the dimer interface as a stick representation. Right: Close-up of the regions around the mutation, showing its interactions with the terminal Y505 residue responsible for stabilizing the agonist conformation. b The PPARγ T475M mutation modulates the structural dynamics of the LDB. Mean structure and atomic fluctuations of the holo PPARγ WT LBD-coactivator (left) and holo PPARγ T475M LBD-coactivator (right) complexes, with the rosiglitazone ligand (in cyan), and the scale of flexibility shown. Bottom: Close-up of the C-terminal H12 helix of the WT and mutant LBDs, as determined from molecular dynamics simulations
