Figure 5
From: Arrestin-1 engineering facilitates complex stabilization with native rhodopsin
Proposed complex formation of the promiscuous arrestin-1 quadruple mutant with P-ROS and ROS* in comparison to the arrestin-1 WT bound P-ROS*. WT arrestin-1 has been shown to need both, electrostatic interactions via the GPCR C-terminal tail, as well as the conformational docking with the GPCR cytoplasmic cavity to form a stable interaction with rhodopsin. The shown data suggest that the arrestin-1 (R171A, T304A, E341A, F375A) quadruple mutant is additionally able to utilize both interactions individually to form a stable rhodopsin–arrestin-1 complex.
