Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1.

ABSTRACT: G-protein-coupled receptor (GPCR) kinases (GRKs) selectively phosphorylate activated GPCRs, thereby priming them for desensitization¹. Although it is unclear how GRKs recognize these receptors^2-4, a conserved region at the GRK N terminus is essential for this process^5-8. Here we report a series of cryo-electron microscopy single-particle reconstructions of light-activated rhodopsin (Rho*) bound to rhodopsin kinase (GRK1), wherein the N terminus of GRK1 forms a helix that docks into the open cytoplasmic cleft of Rho*. The helix also packs against the GRK1 kinase domain and stabilizes it in an active configuration. The complex is further stabilized by electrostatic interactions between basic residues that are conserved in most GPCRs and acidic residues that a

SUBMITTER: Chen Q 

PROVIDER: S-EPMC8607881 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature