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The human metabotropic glutamate receptor 5 transmembrane domain is a homodimeric GPCR that resides in the cellular membrane. This domain is a member of the Class C GPCR family and can further be categorized into the Group I subgroup. As such, the transmembrane domain will signal through a Gq/11 pathway. mGlu5 will bind glutamate to the extracellular Venus flytrap domain and the signal will be transduced across the membrane to a heterotrimeric G protein, which will ultimately lead to calcium release and activation of PKC. This will elicit a excitory post-synaptic repose and modulate long term potentiation. Human metabotropic glutamate receptor 5 is found throughout the central nervous system. Areas containing high concentrations of this protein are often involved involved in emotions and higher cognition. The localization of mGlu5 in the CNS and the presence of multiple domains makes mGlu5 a possible target for treating schizophrenia, Fragile X, depression, anxiety,and Alzheimer's disease.

Discovery

The mGlu famicly of receptors was the first of the Class C GPCR to be extensively studied. The first regions of the protein crystallized and studied were the Venus fly trap domain and the cystiene-rich domain on the extracellular region of the receptor. The hydrophobic nature and flexibility of the transmembrane domain made it difficult to crystalize. It was not until when the Human metabotropic glutamate receptor 5 transmembrane domain crystallized and elucidated a structure of the transmembrane domain.

Structure

Figure Legend

Extracellular Domain

Binding Pocket

Ionic Locks

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Function and Pathway

Disease

Fragile X

Parkinsons

Relevance

Structural highlights

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