Abstract
There is increasing evidence that G protein-coupled receptors form oligomers and that this might be important for their function. We have studied this phenomenon for the D2 dopamine receptor and have shown—using a variety of biochemical and biophysical techniques—that this receptor forms dimers or higher-order oligomers. Using ligand-binding studies, we have also found evidence that this oligomer formation has functional relevance. Thus, for the receptor expressed in either CHO cells or Sf 9 insect cells, the binding properties of several radioligands (in saturation, competition, and dissociation assays) do not conform to those expected for a monomeric receptor with a single binding site. We propose that the receptors exist in oligomers with homotropic and heterotropic negatively cooperative interactions between ligands.
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Strange, P.G. Oligomers of D2 dopamine receptors. J Mol Neurosci 26, 155–160 (2005). https://doi.org/10.1385/JMN:26:2-3:155
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DOI: https://doi.org/10.1385/JMN:26:2-3:155