Fig. 2: Unique structure features and binding pocket.
From: Activation and signaling mechanism revealed by GPR119-Gs complex structures
a The second extracellular loop (ECL2) of GPR119 in an extracellular view. ECL2 is colored blue. The phenylalanines and disulfide bonds are shown as green and yellow sticks, respectively. b GPR119 displays a noncanonical consensus scaffold of non-covalent contacts in contrast to that of canonical class A GPCRs. GPR119 (pink, this study) and β2AR (gray, PDB ID: 3SN6) are superimposed with the Cαs of the 5 non-conserved inter-TM contacts shown as yellow and green spheres, linked by sticks, respectively. c The one-amino acid shift of the conserved Pro1765.50 results in an outward bulge of TM5. GPR119 (pink, this study) and β2AR (gray, PDB ID: 3SN6) are superimposed with Pro5.50 shown as stick. The black arrow shows the one-amino acid shift of the conserved Pro5.50. d Ligand binding pocket comparison between MBX-2982-GPR119 (this study) and IRL2500-ETBR (PDB ID:6k1q). GPR119, MBX-2982, ETBR, and IRL2500 are colored orange, green, light yellow, and magenta, respectively. e, f Cutaway view showing AR231453 (cyan) in the ligand binding pocket of GPR119 (pink) (e) and MBX-2982 (green) in that of GPR119 (orange) (f). The three functional compartments, an activation cavity, a stacking gate, and an extracellular cavity are indicated.
