Fig. 1: Structure basis of P2Y14 activation.
From: Structural insights into ligand recognition and activation of human purinergic receptor P2Y14
a Schematic representation of P2Y14-mediated activation of downstream Gi protein signaling pathways in response to various ligands. b Chemical structures of the endogenous agonists used in this study. The chemical groups of endogenous agonists were represented in distinct colors. c Agonist potency on G-protein signaling in P2Y14, analyzed using a calcium-induced luciferase accumulation assay. Data are shown as the mean ± SEM. from three independent measurements. d Cryo-EM density maps of the UDPG-, UDPGA-, and NADH-bound P2Y14–Gi complexes. e–g Interactions between UDPG (pink) with P2Y14 (blue) (e), UDPGA (violet) with P2Y14 (strong cyan) (f), and NADH (cyan) with P2Y14 (purple) (g). h Structural comparison between the active P2Y14 (strong cyan) and inactive P2Y12 (dark orange). i Structural rearrangement of the PIF triad and toggle switch during P2Y14 activation. j Structural rearrangement of the E/DRY and NPXXY motifs during P2Y14 activation. k Detailed interactions of P2Y14 with the α5-helix of Gi in the UDPGA-bound P2Y14 structure. Hydrogen-bonding interactions are shown with green dashed lines, and ionic interactions are shown with pink dashed lines.
