Sequential inter- and intrasubunit rearrangements during activation of dimeric metabotropic glutamate receptor 1. Closed state of both binding domains of homodimeric mGlu receptors is required for full activity. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Organization and functions of mGlu and GABA B receptor complexes. Metabotropic glutamate receptors: physiology, pharmacology, and disease. Interactions between the cysteine-rich domains and the second extracellular loops of the receptor enable the rigid-body repositioning of the 7-transmembrane domains, which come into contact with each other to initiate signalling. Our results show that agonist binding at the Venus flytraps leads to a compaction of the intersubunit dimer interface, thereby bringing the cysteine-rich domains into close proximity. Here, using a combination of X-ray crystallography, cryo-electron microscopy and signalling studies, we present a structural framework for the activation mechanism of metabotropic glutamate receptor subtype 5. Spectroscopic studies show that signalling is a dynamic process, in which large-scale conformational changes underlie the transmission of signals from the extracellular Venus flytraps to the G protein-coupling domains-the 7-transmembrane domains-in the membrane. They form obligate dimers and possess extracellular ligand-binding Venus flytrap domains, which are linked by cysteine-rich domains to their 7-transmembrane domains.

Metabotropic glutamate receptors are family C G-protein-coupled receptors.

2ef7 map thermostat activation lock