| Title: | The activation mechanism of class-C G-protein coupled receptors |
| Author(s): | Pin JP; Kniazeff J; Goudet C; Bessis AS; Liu J; Galvez T; Acher F; Rondard P; Prezeau L; |
| Address: | "Lab. of Functional Genomic, Dept. of Molecular Pharmacology, CNRS UPR-2580, 141 rue de la Cardonille, 34094 Montpellier Cedex 5, France. jppin@ccipe.cnrs.fr" |
| DOI: | 10.1016/j.biolcel.2004.03.005 |
| ISSN/ISBN: | 0248-4900 (Print) 0248-4900 (Linking) |
| 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" |
| Keywords: | "Allosteric Site Animals Glutamic Acid/chemistry Humans Ligands Models, Biological Phylogeny Protein Binding Protein Structure, Tertiary Receptors, G-Protein-Coupled/chemistry/*metabolism/*physiology gamma-Aminobutyric Acid/chemistry;" |
| Notes: | "MedlinePin, J-P Kniazeff, J Goudet, C Bessis, A-S Liu, J Galvez, T Acher, F Rondard, P Prezeau, L eng Review England 2004/06/23 Biol Cell. 2004 Jun; 96(5):335-42. doi: 10.1016/j.biolcel.2004.03.005" |
