Fig. 5: In contrast to GPR61, GPR161, and β2AR, GPR174 adopts a non-canonical Gs coupling mode. | Nature Communications

Fig. 5: In contrast to GPR61, GPR161, and β2AR, GPR174 adopts a non-canonical Gs coupling mode.

From: Specific binding of GPR174 by endogenous lysophosphatidylserine leads to high constitutive Gs signaling

Fig. 5: In contrast to GPR61, GPR161, and β2AR, GPR174 adopts a non-canonical Gs coupling mode.The alternative text for this image may have been generated using AI.

a Structural overlay of β2AR‒Gs and GPR174‒Gs complexes from the side view. b Comparison of structures of inactive β2AR (PDB: 2RH1), active β2AR (PDB: 3SN6), active μOR (PDB: 6DDE) and active GPR174 in two orthogonal views. c Structural overlay of GPR174‒Gs, CCK1R‒Gs (PDB: 7MBX), GPR52‒Gs (PDB: 6LI3), and NK1R‒Gs (PBD: 7RMI) complexes from the cytoplasmic view. All these complexes adopt a non-canonical Gs coupling mode where the hook of Gαs is distorted and the outward movement of TM6 is less pronounced compared to β2AR. α5 of Gαs is shown with other regions hidden.

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