Fig. 7
From: Defining a conformational ensemble that directs activation of PPARγ
Co-regulator-binding shifts the helix 12 conformational ensemble. a Deconvoluted 19F NMR spectra of apo PPARγC313A,K502C-BTFA and PPARγK502C-BTFA bound to GW1929 or T0070907 in the absence and presence of MED1 coactivator or NCoR corepressor peptides. The percent of total signal area found in the left sharp peak is shown for T0070907 and GW9662 spectra. The small sharp peak at ~−83.3 ppm is free BTFA. b Mean-weighted chemical shift values from the plots in a. c Fraction of the total peak areas in the four colored boxed regions in a, which roughly correspond to the clustered spectral regions from Fig. 2; with the two middle regions corresponding to the two peaks observed for apoprotein. Agonist-bound PPARγ is changed little by MED1 binding, whereas NCoR binding changes the spectrum drastically and vice versa for inverse-agonist (T0070907)-bound PPARγ. *SMRT-induced mean chemical shift in GW1929-bound PPARγK502C-BTFA is the same as NCoR. These experiments were performed once
