G protein-coupled receptor heteromerization: a role in allosteric modulation of ligand binding.

ABSTRACT: It is becoming increasingly recognized that G protein-coupled receptors physically interact. These interactions may provide a mechanism for allosteric modulation of receptor function. In this study, we examined this possibility by using an established model system of a receptor heteromer consisting of μ and δ opioid receptors. We examined the effect of a number of μ receptor ligands on the binding equilibrium and association and dissociation kinetics of a radiolabeled δ receptor agonist, [(3)H]deltorphin II. We also examined the effect of δ receptor ligands on the binding equilibrium and association and dissociation kinetics of a radiolabeled μ receptor agonist, [(3)H][d-Ala(2),N-Me-Phe(4),Gly(5)-ol]-enkephalin ([(3)H]DAMGO). We show that μ receptor ligands are capable of allosterically en

SUBMITTER: Gomes I 

PROVIDER: S-EPMC3102551 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature