Extended Data Figure 4. Disulphide trapping strategy reveals close proximity of residue 235 of the β2V2R and residue 78 at the distal end of the finger loop in βarr1.
a. Structural model of the β2V2R-βarr1 complex depicting the proximity of K235 on the β2V2R and D78 on βarr1. b. Single cysteine insertion mutants of the β2V2R (covering residues 231- 236 ) and βarr1D78C were co-transfected in HEK-293 cells and complex formation was induced by stimulating the cells with an oxidizing agent H2O2 and agonist (Isoproterenol; Iso). Subsequenlty, a co-immunoprecipitation assay was performed using FLAG M2 beads (FLAG-βarr1). Formation of disulphide trapped complex was visualized by Western blotting. c. Quantification of βarr1 in S-S trapped complex from three indepdent experiments with standard error of the mean.