Fig. 6

T0070907 populates a shared conformation with GW9662 and a unique conformation. a Structural location of G399, which is connected to the AF-2 coregulator interaction surface via water-mediated hydrogen bonds to N312 and D313 but does not directly interact with a coregulator peptide bound to the PPARγ LBD (PDB code 2PRG). b Snapshot overlay of [¹H,¹⁵N]-TROSY-HSQC NMR spectra of ¹⁵N-labeled PPARγ LBD (wild-type or R288 mutants) bound to GW9662 or T0070907 shows that the single GW9662-bound G399 peak has similar chemical shift values to one of the two T0070907-bound G399 peaks (state A) whereas state B is uniquely populated by T0070907. The T0070907-bound R288K mutant PPARγ LBD, but not T0070907-bound R288A mutant PPARγ LBD, significantly populates the unique conformation. c Deconvoluted ¹⁹F NMR spectra of PPARγ LBD labeled with BTFA on helix 12 and covalently bound to GW9662 or T0070907