title: Sequential conformational rearrangements dictate the dynamics of class C GPCR activation.
abstract: Heterotrimeric GTP-binding protein (G protein)-coupled receptors (GPCRs) are the largest family of cell surface receptors; they allow cells to respond to a wide range of endogenous and environmental signals. Class C GPCRs represent a discrete group within the GPCR family, with distinct structural characteristics. Receptors belonging to this class--such as γ-aminobutyric acid type B (GABA(B)) receptors or metabotropic glutamate receptors (mGluRs)--form constitutive dimers. However, the conformational changes within such a dimeric receptor that are associated with agonist activation are still not well understood. A study by Hlavackova et al. investigates the role of dimer formation in mGluR1 activation. Using fluorescence resonance energy transfer approaches to assess inter- and intrasubunit conformational changes, the authors present an elegant study that sheds light on the kinetics of domain rearrangements in a class C GPCR upon ligand binding.
authors.affiliation: Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences, and Department of Pharmacology, Monash University, Parkville, Victoria 3052, Australia.
authors.forename: J Robert
authors.initials: JR
authors.lastname: Lane
authors.forename: Meritxell
authors.initials: M
authors.lastname: Canals
mesh_terms: D019281:Dimerization; D031541:Fluorescence Resonance Energy Transfer; D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry*; D018094:Receptors, Metabotropic Glutamate / Q000737:chemistry*
chemical_list: D021122:Protein Subunits; D018094:Receptors, Metabotropic Glutamate