Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors.

ABSTRACT: Arrestins are a small family of proteins that bind G protein-coupled receptors (GPCRs). Arrestin binds to active phosphorylated GPCRs with higher affinity than to all other functional forms of the receptor, including inactive phosphorylated and active unphosphorylated. The selectivity of arrestins suggests that they must have two sensors, which detect receptor-attached phosphates and the active receptor conformation independently. Simultaneous engagement of both sensors enables arrestin transition into a high-affinity receptor-binding state. This transition involves a global conformational rearrangement that brings additional elements of the arrestin molecule, including the middle loop, in contact with a GPCR, thereby stabilizing the complex. Here, we review structural and mutagenesis data

SUBMITTER: Karnam PC 

PROVIDER: S-EPMC8621391 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature