G_i- and G_s-coupled GPCRs show different modes of G-protein binding.

ABSTRACT: More than two decades ago, the activation mechanism for the membrane-bound photoreceptor and prototypical G protein-coupled receptor (GPCR) rhodopsin was uncovered. Upon light-induced changes in ligand-receptor interaction, movement of specific transmembrane helices within the receptor opens a crevice at the cytoplasmic surface, allowing for coupling of heterotrimeric guanine nucleotide-binding proteins (G proteins). The general features of this activation mechanism are conserved across the GPCR superfamily. Nevertheless, GPCRs have selectivity for distinct G-protein family members, but the mechanism of selectivity remains elusive. Structures of GPCRs in complex with the stimulatory G protein, G_s, and an accessory nanobody to stabilize the complex have been reported, providing i

SUBMITTER: Van Eps N 

PROVIDER: S-EPMC5877964 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature