Methods to monitor the quaternary structure of G protein-coupled receptors

FEBS J. 2005 Jun;272(12):2914-25. doi: 10.1111/j.1742-4658.2005.04731.x.


A wide range of approaches has been applied to examine the quaternary structure of G protein-coupled receptors, the basis of such protein-protein interactions and how such interactions might modulate the pharmacology and function of these receptors. These include co-immunoprecipitation, various adaptations of resonance energy transfer techniques, functional complementation studies and the analysis of ligand-binding data. Each of the available techniques has limitations that restrict interpretation of the data. However, taken together, they provide a coherent body of evidence indicating that many, if not all, G protein-coupled receptors exist and function as dimer/oligomers. Herein we assess the widely applied techniques and discuss the relative benefits and limitations of these approaches.

Publication types

  • Review

MeSH terms

  • Animals
  • Biochemistry / methods
  • Dimerization
  • Fluorescence Resonance Energy Transfer / methods
  • Humans
  • Immunoprecipitation / methods
  • Ligands
  • Luminescent Measurements / methods
  • Molecular Biology / methods*
  • Protein Structure, Quaternary*
  • Receptors, G-Protein-Coupled / chemistry*
  • Receptors, G-Protein-Coupled / metabolism


  • Ligands
  • Receptors, G-Protein-Coupled