Reinterpreting anomalous competitive binding experiments within G protein-coupled receptor homodimers using a dimer receptor model.

ABSTRACT: An increasing number of G protein-coupled receptors (GPCRs) have been reported to be expressed in the plasma membrane as dimers. Since most ligand binding data are currently fitted by classical equations developed only for monomeric receptors, the interpretation of data could be misleading in the presence of GPCR dimers. On the other hand, the equations developed from dimer receptor models assuming the existence of two orthosteric binding sites within the dimeric molecule offer the possibility to directly calculate macroscopic equilibrium dissociation constants for the two sites, an index of cooperativity (D_C) that reflects the molecular communication within the dimer and, importantly, a constant of radioligand-competitor allosteric interaction (K_DAB) in competitive a

SUBMITTER: Casado-Anguera V 

PROVIDER: S-EPMC6360119 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature