Conserved Mechanism of Conformational Stability and Dynamics in G-Protein-Coupled Receptors.

ABSTRACT: G-protein-coupled receptors (GPCRs) are transmembrane receptors involved in diverse biological functions. Despite the diversity in their amino acid sequences, class A GPCRs exhibit a conserved structural topology and possibly a common mechanism of receptor activation. To understand how this high sequence diversity translates to a conserved functional mechanism, we have compared the dynamic behavior of eight class A GPCRs comprised of six biogenic amine receptors, adenosine A_2A, and the peptide receptor protease-activated receptor 1. Starting from the crystal structures of the inactive state of these receptors bound to inverse agonists or antagonists, we have performed multiple all-atom MD simulations adding up to several microseconds of simulation. We elucidated the similarities

SUBMITTER: Bhattacharya S 

PROVIDER: S-EPMC5148705 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature