Fig. 2: Phosphopeptides induce arrestin to form an active conformation.
From: Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
a Plots of the distance root mean square deviations (RMSDs) for individual residues between inactive arrestin2 and the V2Rpp-FP/1/3/4/6-7-arrestin2 complexes. The three loops that exhibit major conformational changes in all complexes are highlighted: finger loop, light red; middle loop, light green; and lariat loop, light blue. Arrestin2-V2Rpp-FP, PDB: 4JQI; arrestin2-NTSR1-c, PDB: 6PWC; arrestin2-NTSR1-n, PDB: 6UP7; arrestin2-M2R, PDB: 6U1N; arrestin2-β1AR6P, PDB: 6TKO; arrestin2-V2T, PDB:6NI2. b Similar conformational distortions of the Lariat loop in the V2Rpp-1/3/4/67-arrestin2 complex. c pT360 of V2Rpp-1/3/67 maintained H-bond interactions with residues K294 and R25, similar to V2Rpp-FP. d A different binding mode of V2Rpp-4. V2Rpp-4 lost both the V3 and V4 site interactions. Instead, it formed a phospho-interaction via the identified V3′4′ site. e The solvent accessibilities of several functional regions in arrestin2 in five different phosphopeptides-arrestin2 complex structures (Black circle: arrestin2-V2Rpp-FP, PDB: 4JQI; Blue triangle: arrestin2-V2Rpp-1; green triangle: arrestin2-V2Rpp-3; brown triangle: arrestin2-V2Rpp-4; pink triangle: arrestin2-V2Rpp-6-7). Data are reported as box and whiskers plot, the whiskers show the maximum and the minimum; the box indicates the first and third quartiles; and the line in the box is the median value. The median values are reported next to the boxplot. The different color triangles and circle represent the five different phosphopeptides-arrestin2 complex structures’ averaged for the solvent accessibilities in corresponding regions. Source data are provided in the Source Data file.
