Science Advances

Supplementary Materials

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  • Supplementary Text
  • Fig. S1. Characterization of A2AAR prepared in rHDLs.
  • Fig. S2. Assignments of the resonances from the methionine residues of A2AAR.
  • Fig. S3. Introduction of methionine residues in the cytoplasmic ends of the A2AAR TM regions.
  • Fig. S4. Resonances from methionine residues at the cytoplasmic ends of the A2AAR TM region.
  • Fig. S5. NMR spectra of A2AAR in rHDL(POPC/POPG) at various temperatures.
  • Fig. S6. Lipids used for the reconstitution of A2AAR into rHDLs.
  • Fig. S7. Signaling activity and conformation of A2AAR in rHDL.
  • Fig. S8. Conformational changes in the TM region of A2AAR upon activation.
  • Fig. S9. Conformation of TM6.
  • Table S1. 35S-GTPĪ³S binding to complexes of purified G protein and A2AAR in rHDL(POPC/POPG) with 0, 0.5, 1, and 2 mol% trifluoroethanol (TFE), in the presence of the full agonist.

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