Fig. 5: The Gs engaging model of GPR174.
From: Structural basis of lysophosphatidylserine receptor GPR174 ligand recognition and activation

a TM6/ICL3 junction forms extensive polar interaction with Gαs. b The overall engagement of αH5. Density map was drawn by chimeraX at a map level of 0.08. c The detail of the αH5 head interaction. d A superimposition of αH5 engagements in the context of GPR174. e A detailed comparison of αH5 engagements among GPR174, EP2 (PDB: 7cx2) and β2AR (PDB: 3ns6). f L393 of the aH5 head inserts into hydrophobic pockets formed by residues from TM1,2,7 and H8.