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Comment
. 2023 Oct;33(10):735-736.
doi: 10.1038/s41422-023-00843-x.

Steering G protein activation by mGlu heterodimer

Guillaume Lebon  1
Affiliations
Comment

Steering G protein activation by mGlu heterodimer

Guillaume Lebon. Cell Res. 2023 Oct.
No abstract available

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Figures

Fig. 1
Fig. 1. Schematic model showing allosteric modulation of mGlu heterodimers and G protein activation.
Inactive state Roo displays some diversity with different dimerization modes (modes I, II, III). Glutamate binding induces the closure of one VFT that likely drives the rearrangement of the heterodimer quaternary structure (Rco state). In the intermediate active state structure (Acc), and in the presence of G protein (Acc–G protein), both VFTs bind glutamate and are in closed state but with some differences at the helical bundle interface. The selection of the mGlu subunit that activates the G protein depends on the stability of each subunit in the inactive state and can be pharmacologically modulated by drugs acting either in one of the 7TMs (blue) or at their molecular interface (green).
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