Extended Data Fig. 3: Activation of GPBAR by P395 and INT-777.
From: Structural basis of GPBAR activation and bile acid recognition
a, Diagram of P395 interaction in the ligand binding pocket of GPBAR. The hydrogen bond is depicted as a dashed line. b, The restraint of the hydrophobic pathes forces the folding of P395 into a U-shaped configuration rather than an extended topology, as predicted by previous studies. c, Schematic representation of the chemical structure of INT-777 (4 rings, ring A, B, C and D were designated). d, The INT-777 assumes a flat structure, folding between the ring A and the ring B of its steroid core with an approximately 100 degree. The ring B-D is parallel to TM2. e, The orientation of the INT-777 aligned to the TM2, TM3, TM5, TM6 or TM7 of GPBAR. f, Structural comparison of the INT-777 and the P395 at the GPBAR ligand binding pocket. Colour usage: INT-777, slate; P395, magenta; GPBAR in the INT-777–GPBAR–Gs complex, green; GPBAR in the P395–GPBAR–Gs complex, slate.
