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The activation mechanism of class‐C G‐protein coupled receptors
Author(s) -
Pin J.P,
Kniazeff J,
Goudet C,
Bessis A.S,
Liu J,
Galvez T,
Acher F,
Rondard P,
Prézeau L
Publication year - 2004
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/j.1768-322x.2004.tb01423.x
Subject(s) - g protein coupled receptor , rhodopsin like receptors , heterotrimeric g protein , receptor , class c gpcr , biology , g protein , agonist , microbiology and biotechnology , biochemistry , metabotropic glutamate receptor , metabotropic receptor
Summry— 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 γ‐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.