Fig. 1
From: Cryo-EM structure of activated bile acids receptor TGR5 in complex with stimulatory G protein
Structural and biochemical studies of TGR5-Gs complex. a cAMP response of full-length and truncated TGR5 with compounds 23H, INT77, CA, LCA, and DLCA. cAMP responses are shown as percentages of the maximum response of each ligand. The data represent means ± S.E.M. (n = 3–5) and most error bars are within the dimensions of the data points. b Cryo-EM structure of TGR5-Gs complex. TGR5, Gαs, Gβ, Gγ, Nb35, and 23H are shown in blue, wheat, light blue, light green, grey, and yellow, respectively. c Residues in TGR5 that involve in 23H binding. Density of 23H is shown in yellow. Residues that might involve in 23H binding are shown in pink. d cAMP responses of mutant TGR5. These mutational TGR5 reduced agonist potency by two order compared with wild-type. The corresponding pEC50 is shown in supplementary Table 2. cAMP responses are shown as percentages of the maximum response of the WT. The data represent means ± S.E.M. (n = 3–5). WT data were not shown on panel b (right panel) because all the mutations were tested at the same time. e Comparisons of active TGR5 (blue) with active (grey) and inactive (wheat) β2AR. f Interface of TGR5 with Gs protein. Residues in TGR5 are shown in blue and residues in Gαs are shown in wheat. D312 in Gβ is shown in light blue
