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. Author manuscript; available in PMC: 2021 Sep 17.
Published in final edited form as: Cell. 2020 Sep 17;182(6):1574–1588.e19. doi: 10.1016/j.cell.2020.08.024

Figure 6. HTR2A Couples Efficiently to Gq-Family Members In Vitro.

Figure 6.

(A)Shown is an alignment of the HTR2A-Gq (green and olive, respectively) and the M1-G11 (lavender and pink, respectively) interface at the tip of the α5 helix of the respective Gα subunits. As depicted, V359H5.26 unde rgoes a 4.8 Å shift in HTR2A compared with M1 while Y356H5.23 is shifted 2.9 Å relative to M1.

(B) Shows a comparison of HTR2A-Gq with the HTR1B-Go (yellow and gray, respectively) showing that the HTR2A Y354H5.26 cognate residue V246H5.26 is shifted up 10.9 Å.

(C) Shows a heatmap of the relative efficacy for selected agonists at HTR2A versus a reference agonist for 14 distinct Gα subunits.

(D)Shows concentration-response curves (N = 3 biological replicates each) for the 14 Gα subunits in 7C along with controls for the Gz study.

See also Table S7.