Extended Data Fig. 6: Structural conformation changes of solved agonist- and antagonist-bound class A GPCRs.

a, The pattern of r.m.s.d. values of transmembrane helices between agonist- and antagonist-bound class A GPCR structures. The structures used for analysis are the same as described in Extended Data Table 3. b, Measurement of the degree of helix VI bending observed in class A GPCRs structures. All structures were superimposed onto inactive-state β₂-adrenergic receptor by UCSF Chimera. The direction of helices VI were defined by vectors η_i which starts from the centre of C_α of residues 6.45–6.48 to the centre of C_α of residues 6.29-30–6.32-33. The two vectors η₀ and η₁ of helices VI in the inactive-state and active-state β₂-adrenergic receptor were selected as reference to form a plane α. The vector η_i of helix VI of other structure was projected to the plane α as a new vector η_i’. The bending angle of each helix VI was then defined by the angle between η_i’ and η₀. The structures are: ET_B (PDB code 5GLH), β₁-adrenergic receptor (PDB code 2Y02), P_2Y12 (PDB code 4PXZ), β₂-adrenergic receptor (PDB code 3PDS), FFA1 (PDB code 4PHU), 5HT_2B (PDB code 4IB4), 5HT_1B (PDB code 4IAR), Rho (PDB code 2HPY), A_2A (PDB code 3QAK), NTS₁ (PDB code 4BUO), CB₁ (bound to AM11542; PDB code 5XRA), μ-opioid receptor + nanobody (NB) (PDB code 5C1M), Rho + NB (PDB code 2×72), Rho + arrestin (PDB code 4ZWJ), M2R + NB (PDB code 4MQS), β₂-adrenergic receptor + NB (PDB code 4LDL), A_2A + mini-G_s (PDB code 5G53), β₂-adrenergic receptor + G_s (PDB code 3SN6).