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Structural insights into the activation of metabotropic glutamate receptors
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Journal Article
Structural insights into the activation of metabotropic glutamate receptors
2019
Overview
Metabotropic glutamate receptors are family C G-protein-coupled receptors. They form obligate dimers and possess extracellular ligand-binding Venus flytrap domains, which are linked by cysteine-rich domains to their 7-transmembrane domains. 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. 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. 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. 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.
The activation mechanism of metabotropic glutamate receptor subtype 5, a member of the family C G-protein-coupled receptors, is characterized by a combination of cryo-electron microscopy, crystallography and signalling studies.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 101/28
/ 13/31
/ 38
/ 82/83
/ 96/10
/ 96/106
/ 96/109
/ 96/95
/ Binding
/ Cysteine
/ Dimers
/ Glutamic acid receptors (metabotropic)
/ Humanities and Social Sciences
/ Humans
/ Ligands
/ Metabotropic glutamate receptors
/ Methods
/ Proteins
/ Receptor, Metabotropic Glutamate 5 - chemistry
/ Receptor, Metabotropic Glutamate 5 - metabolism
/ Receptor, Metabotropic Glutamate 5 - ultrastructure
/ Science
