Fig. 6: Mutational analysis of amino acid residues within the ligand binding pocket of REV-ERBα.
From: Structural basis of synthetic agonist activation of the nuclear receptor REV-ERB
a Results of a two-hybrid reporter assay (Gal4-FL REV-ERBα/NCoR1-VP16) assay illustrating the effects of mutation of amino acid residues that interact with STL1267 within the ligand binding pocket. (WT ▾, F497A ●, F443A ■, L480A ▲, F439A ♦, F484A ○, F488A □). Each point in the biochemical and cell-based experiments represent triplicate determinations and experiments were typically repeated three times. Data are presented as mean ± SEM. b Overlay of the ligand binding pockets of REV-ERBα/STL1267/NCoR ID1 complex before (green) and after (blue) the MD simulations. c Distance probability distribution for STL1267 and selected amino acid residues (F497A yellow, F443A red, L480A black, F439A purple, F484A blue, F488A green).
