Fig. 3

Interaction modes of the residues at positions 2.50 and 7.49 and functional assays of NK1R mutants. a Strong hydrogen-bond interaction between D78^2.50 and N301^7.49 (2.8 Å) and weak interaction between N78^2.50 and N301^7.49 (3.5 Å). Two NK1R structures are shown in cartoon representation and colored green (E78^2.50D mutant) and cyan (E78^2.50N mutant). The residues at positions 2.50 and 7.49 are shown as sticks. b SP-induced cAMP accumulation measurements of the wild-type (WT) NK1R and the mutants E78^2.50D, N301^7.49Q, E78^2.50D/N301^7.49Q, E78^2.50N, N301^7.49E, and E78^2.50N/N301^7.49E. Dose–response curves were generated from at least three independent experiments performed in triplicate. Data shown are mean ± s.e.m. See Supplementary Table 3 for detailed statistical evaluation. c SP-induced IP1 accumulation of the WT NK1R and the mutants E78^2.50D, N301^7.49Q, E78^2.50D/N301^7.49Q, E78^2.50N, N301^7.49E, and E78^2.50N/N301^7.49E. Dose–response curves were generated from at least three independent experiments performed in triplicate or duplicate. Data shown are mean ± s.e.m. See Supplementary Table 2 for detailed statistical evaluation. Source data for Fig. 3b, c are provided as a Source Data file