Fig. 5: Functional impacts of inverse agonists on pathogenic mutant PPARγ.
From: Structural determinants of non-covalent PPARγ inverse agonism and their therapeutic implications
A Structural mapping of disease-relevant mutations within PPARγ-LBD (adapted from PDB:8B8X). PPRE reporter activity assays using PPARγ harboring B Y501A (red in A), C F310A (green), D A261E (sky-blue), and E F388L (blue) were shown as fold change relative to WT-PPARγ receptor activity under DMSO control (Fig. 2A). All assays were conducted in HEK293T cells in the presence of 1 μΜ compound treatment for 24 h. Dashed lines indicate SR10171 reference level. Colors of data points and error bars represent the groups based on regiochemistry. Colored bars above compound names denote the functional classification (green: non-IA, blue: partial-IA, purple: full-IA). Data represent the mean ± SD from three biological replicates (each has five technical replicates) with statistical significance over DMSO in each mutant group. *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, ****p ≤ 0.0001. One-way ANOVA corrected by Tukey’s multiple comparison.
