The World of GPCR dimers - Mapping dopamine receptor D₂ homodimers in different activation states and configuration arrangements.

ABSTRACT: G protein-coupled receptors (GPCRs) are known to dimerize, but the molecular and structural basis of GPCR dimers is not well understood. In this study, we developed a computational framework to generate models of symmetric and asymmetric GPCR dimers using different monomer activation states and identified their most likely interfaces with molecular details. We chose the dopamine receptor D₂ (D₂R) homodimer as a case study because of its biological relevance and the availability of structural information. Our results showed that transmembrane domains 4 and 5 (TM4 and TM5) are mostly found at the dimer interface of the D₂R dimer and that these interfaces have a subset of key residues that are mostly nonpolar from TM4 and TM5, which was in line with experiment

SUBMITTER: Bueschbell B 

PROVIDER: S-EPMC10497915 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature