The Role of Individual Residues in the N-Terminus of Arrestin-1 in Rhodopsin Binding.

ABSTRACT: Sequences and three-dimensional structures of the four vertebrate arrestins are very similar, yet in sharp contrast to other subtypes, arrestin-1 demonstrates exquisite selectivity for the active phosphorylated form of its cognate receptor, rhodopsin. The N-terminus participates in receptor binding and serves as the anchor of the C-terminus, the release of which facilitates arrestin transition into a receptor-binding state. We tested the effects of substitutions of fourteen residues in the N-terminus of arrestin-1 on the binding to phosphorylated and unphosphorylated light-activated rhodopsin of wild-type protein and its enhanced mutant with C-terminal deletion that demonstrates higher binding to both functional forms of rhodopsin. Profound effects of mutations identified lysine-15 as the

SUBMITTER: Vishnivetskiy SA 

PROVIDER: S-EPMC11765510 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature