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. 2023 Jun 6;14:3271. doi: 10.1038/s41467-023-38985-6

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© The Author(s) 2023, corrected publication 2023

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Fig. 6 — a Cytoplasmic cavity formed by TM3, TM5, TM6, and TM7 of GPR84, with the C-terminal α5 helix of the Gα_i inserted. b Key interactions between the extended TM5 and Gα_i residues. c Dose-response curves of LY237 in inducing Gα_i recruitment to GPR84 with various mutations. Data are shown as mean ± S.E.M. from a minimum of three technical replicates, which performed in triplicates. The representative dose-response curves are shown. d, e Hydrophobic network (d) and polar interactions (e) between GPR84 and α5 helix of Gα_i. f Hydrophobic packing formed by residues from TM2-4 and ICL2. g Interactions formed by ICL2 and αN of Gα_i protein. Source data are provided as a Source data file.