Allosteric functioning of dimeric class C G-protein-coupled receptors.
Whereas most membrane receptors are oligomeric entities, G-protein-coupled receptors have long been thought to function as monomers. Within the last 15 years, accumulating data have indicated that G-protein-coupled receptors can form dimers or even higher ordered oligomers, but the general functional significance of this phenomena is not yet clear. Among the large G-protein-coupled receptor family, class C receptors represent a well-recognized example of constitutive dimers, both subunits being linked, in most cases, by a disulfide bridge. In this review article, we show that class C G-protein-coupled receptors are multidomain proteins and highlight the importance of their dimerization for activation. We illustrate several consequences of this in terms of specific functional properties and drug development.
Pin
J-P
JP
Institut de Génomique Fonctionnelle, Montpellier, France. jppin@ccipe.cnrs.fr
Kniazeff
J
J
Liu
J
J
Binet
V
V
Goudet
C
C
Rondard
P
P
Prézeau
L
L
D000818:Animals; D019281:Dimerization; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry* / Q000378:metabolism*
D043562:Receptors, G-Protein-Coupled