Related Experiment Video
Updated: Feb 18, 2026

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
Published on: August 17, 2022
The activation mechanism of class-C G-protein coupled receptors
J-P Pin1, J Kniazeff, C Goudet
1Lab. of Functional Genomic, Dept. of Molecular Pharmacology, CNRS UPR-2580, 141 rue de la Cardonille, 34094 Montpellier Cedex 5, France. jppin@ccipe.cnrs.fr
Abstract:
Class-C G-protein coupled receptors (GPCRs) represent a distant group among the large family of GPCRs. This class includes the receptors for the main neurotransmitters, glutamate and gamma-aminobutyric acid (GABA), and the receptors for Ca(2+), some taste and pheromone molecules, as well as some orphan receptors. Like any other GPCRs, class-C receptors possess a heptahelical domain (HD) involved in heterotrimeric G-protein activation, but most of them also have a large extracellular domain (ECD) responsible for agonist recognition and binding. In addition, it is now well accepted that these receptors are dimers, either homo or heterodimers. This complex architecture raises a number of important questions. Here we will discuss our view of how agonist binding within the large ECD triggers the necessary change of conformation, or stabilize a specific conformation, of the heptahelical domain leading to G-protein activation. How ligands acting within the heptahelical domain can change the properties of these complex macromolecules.
More Related Videos
Related Concept Videos
Activation and Inactivation of G Proteins
G-protein Coupled Receptors
Transducer Mechanism: G Protein–Coupled Receptors
GPCRs are also called heptahelical,...
G Protein-coupled Receptors
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G-Protein Gated Ion Channels
Sensory...
GPCRs Regulate Adenylyl Cylase Activity

