Fig. 5: DAG and MAG bind to the L2 site for channel activation.

a Close-up view of DAG at the L2 site. The mutated amino acids on hTRPC3 are shown as sticks. DAG is colored in green. TRPC3 is colored in blue. b The ratio of peak currents activated by CCh and GSK1702934A in wild-type, E603A, K607A, and V637A under whole-cell mode at −60 mV. The calculation method for the activation current is described in detail in Supplementary Fig. 10. The number of biological replicates in each group is indicated below the genotype. The data are shown as the mean ± SD. The data were analyzed using Brown–Forsythe and Welch ANOVA tests, and the multiple comparisons between each group were analyzed using Dunnett’s T3 multiple comparisons tests with p-values indicated above the corresponding groups. Source data are provided as a Source Data file. c The ratio of peak currents activated by OAG and GSK1702934A in wild-type, E603A, K607A, and V637A under whole-cell mode at −60 mV. The calculation, annotation, and statistical analyses were identical to those described in (b). Source data are provided as a Source Data file. d The ratio of peak currents activated by CCh and 4n in wild-type, E603A, K607A, and V637A under whole-cell mode at −60 mV. The calculation, annotation, and statistical analyses were identical to those described in (b). Source data are provided as a Source Data file. e The ratio of peak currents activated by OAG and 4n in wild-type, E603A, K607A, and V637A under whole-cell mode at −60 mV. The calculation, annotation, and statistical analyses were identical to those described in (b). Source data are provided as a Source Data file. f Chemical structures of DAG, OAG, 1-MOG, and 2-MOG. g–i. Macroscopic currents of wild-type hTRPC3/6/7 recorded in the whole-cell mode. Zero current is indicated by a dashed line. The duration of ligand application is indicated by a solid line above. Source data are provided as a Source Data file.