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Cryo-EM studies of mGlu2 have yielded adequate structures that have acted as maps to aid in producing a better structural understanding of the inactive and active states of mGlu2 (Lin). The overall structure of the mGlu2 is composed of 3 main parts: a ligand binding Venus FlyTrap Domain(VFT), followed by a Cysteine Rich Domain linker to the Transmembrane Domain that contains 7 alpha helices (7TM) on both the alpha and beta chains that aid in the binding of the G-Protein. Class C CPCRs such as mGlu2, are activated by their ability to form dimers. MGlu2 is a homodimer which is imperative to the receptor’s ability to relay signals induced by glutamate from the extracellular domain(ECD) to its transmembrane domain(TMD). The homodimer of mGlu2 contains an alpha chain and a beta chain. Occupation of both ECDs with the agonist, glutamate, is necessary for a fully active mGlu2. However, only one chain in the dimer is responsible for activation of the G-protein, this suggests an asymmetrical signal transduction mechanism for mGlu2.