Abstract

Metabotropic glutamate receptors (mGluRs) are an important family of class C G protein-coupled receptors (GPCRs) characterized by a large extracellular ligand-binding domain (LBD) and a constitutive dimeric arrangement in the cell membrane. While the role of inter-LBD conformational dynamics in mGluR dimerization and activation has been extensively studied, the contribution of the transmembrane domains (TMDs) has only recently been explored using single molecule subunit counting experiments and inter-TMD fluorescence resonance energy transfer (FRET) measurements in living cells.

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