Figure 6
From: Arrestin-1 engineering facilitates complex stabilization with native rhodopsin
Comparison between possible electrostatic interactions of R171 in the inactive (1cf1, β confomer) and active (5w0p) arrestin-1 structures. On the left, the inactive conformation of arrestin-1 is shown29, featuring the modelled distal C-terminal tail in gold. The close-up view above indicates the proposed locations as well as orientations for charged, C-terminal amino acids in a 10 Å radius around R171. The rhodopsin C-terminal tail and the resolved phosphorylated residues are shown in teal, as elucidated in the crystal structure26.
