Extended Data Fig. 10: Structural comparison of active features and G protein coupling in TAS2R14.
From: Bitter taste TAS2R14 activation by intracellular tastants and cholesterol
(a-c) Structural comparison of key motifs related to activation in TAS2R14 and TAS2R46. Trp3.32 and toggle switch residues (a), HS/P7.50FIL and FY3.50L (b) and Trp3.41 residue (c), respectively. (d) Binding mode between TAS2R14 and Gαg in AA150µM-TAS2R14-Gg structure. (e) Binding mode between TAS2R14 and Gαg in 28.1150µM-TAS2R14-Gg structure. (f) Structural comparison of TM6 and ligand binding poses in AA150µM-TAS2R14-Gg and 28.1150µM-TAS2R14-Gg structures. (g) Structure comparison of the miniGαs/gust and Gαg binding modes in TAS2R14. AA150µM-TAS2R14-miniGs/gust and AA150µM-TAS2R14-Gg complex structures are used for analysis. (h) Structure comparison of the Gαi binding modes in TAS2R14 and CB1. (i) Diagram of the contacts between Gαg and TAS2R14 and Gαi1 and TAS2R14, respectively.