Fig. 4: Comparison of the agonist- and antagonist-bound LPA₁ structures.

a–d Superimposition of the CpY- and antagonist-bound LPA₁ structures, colored aquamarine and gray (PDB 4Z34), respectively, a viewed from the membrane plane. b Structural changes of the intramolecular interactions induced by agonist binding. c Rearrangements of the central hydrophobic core and d the P^5.50I^3.40F^6.44 motifs and movement of TM6. e Superimposition of the CpY-, LPA-, and ONO-0740556-bound LPA₁ structures, colored aquamarine and blue (PDB 7TD0), and orange (PDB 7YU3), respectively. f Changes in EC₅₀ and Emax of NanoBiT-G-protein dissociation assays due to the W210^5.43A mutation are shown as means ± s.e.m. from three independent experiments. The W210^5.43A mutant completely lost the response for ONO-0740556. g Interaction of CpY with W(F)271^6.48 in WT and W271F mutant. W271^6.48F is a predicted structure with a residue substitution. CpY and F267^6.44 and W(F)271^6.48 residues are represented by stick models and cpk models. h Changes in EC₅₀ of NanoBiT-G-protein dissociation assays due to the W271^6.48F mutation are shown as means ± s.e.m. from three independent experiments.