Fig. 3 | Nature Communications

Fig. 3

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

Fig. 3

Conformational change of arrestins depend on phosphorylation pattern. a Limited trypsin digest of arrestin-1, -2 and -3 in presence of non- (0P) and fully phosphorylated (7P) phosphopeptide analogs of the rhodopsin C-terminus. The presence of fully phosphorylated peptide resulted in a change of the digestion pattern from three to two bands in comparison to nonphosphorylated peptide for arrestin-1 and -3. The digestion of arrestin-2 always resulted in two bands with similar molecular weight as arrestin-1/-3 independent of which peptide was present. However, digestion was accelerated in the presence of fully phosphorylated peptide as compared to nonphosphorylated peptide. b Limited trypsin digestion of arrestin-1 in the presence of different tri-phosphorylated peptides. Peptide-induced conformational changes in arrestin-1 are indicated by a change in the digest pattern (green boxes) (Source data are provided as a Source Data file.)