Characteristic structural difference between inactive and active states of orexin 2 receptor determined using molecular dynamics simulations.

ABSTRACT: To investigate the dynamics of the orexin 2 receptor, which is a class A G protein-coupled receptor, we recently performed several microsecond-scale molecular dynamics simulations of the wild-type protein, of a mutant that stabilizes the inactive state, and of constitutively active mutants of the class A G protein-coupled receptors. Herein, we review the results of these molecular dynamics simulations of the orexin 2 receptor. In these simulations, characteristic conformational changes were observed in the V309^6.40Y mutant. The conformational changes were related to the outward movement of the transmembrane helix 6 and the inward movement of the transmembrane helix 7, which are common structural changes in the activation of G protein-coupled receptors. The index for the quantita

SUBMITTER: Yokoi S 

PROVIDER: S-EPMC8921386 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature