Fig. 2 | Nature Communications

Fig. 2

From: Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation

Fig. 2

Different phosphorylation patterns have varying abilities to bind arrestins. a Sequence of the bovine rhodopsin C-terminus and schematic illustration of the phosphorylation and charge pattern. In the sequence, potential phosphorylation sites are yellow, and negatively charged acidic residues are blue. In the schematic, the negatively charged patch is blue, nonphosphorylated sites are white, and phosphorylated sites are red. The shapes of the phosphorylation sites indicate their different functions, which were assigned in this study. b Peptides that did not show specific binding or very weak binding to any tested arrestin isoform. c Kd values of all specific binders determined by fluorescence anisotropy for arrestin-1, -2, and -3. Statistical analysis was performed by ANOVA analysis and these values are reported in Supplementary Information Tables 1, 2 and 3. d Fluorescence anisotropy arrestin-1 binding curves of nonphosphorylated peptide 0P (different shades of blue) and the tri-phosphorylated peptide 3Pd (different shades of green). Each titration was repeated three or four times. Fits of the individual binding curves were used to obtain error bars shown in part (c) and Table 2 (Source data are provided as a Source Data file.)