ArticleFrontiers in molecular biosciences2020
Exploring the Activation Mechanism of the mGlu5 Transmembrane Domain.
Article in Frontiers in molecular biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Delineating the stepwise millisecond allosteric activation mechanism of the class C GPCR dimer mGlu5.Nature communications · 2024Article
- Photoswitchable positive allosteric modulators of metabotropic glutamate receptor 4 to improve selectivity.iScience · 2024Article
- Structural and Biophysical Mechanisms of Class C G Protein-Coupled Receptor Function.Trends in biochemical sciences · 2020Review
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Authors and funding
4 authors.
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Abstract
As a class C GPCR and regulator of synaptic activity, mGlu5 is an attractive drug target, potentially offering treatment for several neurologic and psychiatric disorders. As little is known about the activation mechanism of mGlu5 at a structural level, potential of mean force calculations linked to molecular dynamics simulations were performed on the mGlu5 transmembrane domain crystal structure to explore various internal mechanisms responsible for its activation. Our results suggest that the hydrophilic interactions between intracellular loop 1 and the intracellular side of TM6 have to be disrupted to reach a theoretically active-like conformation. In addition, interactions between residues that are key for mGlu5 activation (Tyr659
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