Supplementary Materials

This PDF file includes:

  • Fig. S1. D2R-WT and D2R mutants express to a similar extent using transient transfection.
  • Fig. S2. Other D2R agonists exhibit G protein bias at the D2R-F1895.38A.
  • Fig. S3. Compound CAB02-110 is a partial agonist at both G protein activation and β-arrestin recruitment.
  • Fig. S4. Rotigotine- and apomorphine-stimulated internalization of the D2-WT and D2R-F1895.38A.
  • Fig. S5. The β2R-Y1995.38A exhibits G protein bias with different agonists.
  • Fig. S6. Partial agonist stimulation of β2R-mediated Gs activation and β-arrestin recruitment.
  • Fig. S7. Distribution of distance between the oxygen of Tyr5.38 side-chain hydroxyl and the backbone oxygen atom of Thr4.56 in the β2R-WT.
  • Fig. S8. IL2 moves downward in the β2R-Y1995.38A mutant.
  • Table S1. β-Arrestin–BRET and Go BRET signaling by D2R-WT and D2R mutants.
  • Table S2. Affinity constants (Ki values) for MLS1547 and dopamine binding to D2R-WT and D2R mutants.
  • Table S3. β-Arrestin recruitment and regulation of cAMP signaling by D2R-WT and D2R-F1895.38A.
  • Table S4. β-Arrestin and Go BRET signaling for D2R-WT and D2R-F1895.38A in response to full D2R agonists.
  • Table S5. β-Arrestin–BRET recruitment for D2R-WT and various mutants at the Phe1895.38 position.
  • Table S6. β-Arrestin– and G protein–mediated signaling by WT and 5.38 mutant D3R, D4R, β2R, and V2R.
  • Table S7. Summary of MD simulations.
  • Table S8. β2R–BI-167107 interacting residues.

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