| Autor: |
Krishna Kumar, Kaavya, Wang, Haoqing, Habrian, Chris, Latorraca, Naomi R., Xu, Jun, O’Brien, Evan S., Zhang, Chensong, Montabana, Elizabeth, Koehl, Antoine, Marqusee, Susan, Isacoff, Ehud Y., Kobilka, Brian K. |
| Zdroj: |
Nature; May2024, Vol. 629 Issue 8013, p951-956, 6p |
| Abstrakt: |
Metabotropic glutamate receptors belong to a family of G protein-coupled receptors that are obligate dimers and possess a large extracellular ligand-binding domain that is linked via a cysteine-rich domain to their 7-transmembrane domain1. Upon activation, these receptors undergo a large conformational change to transmit the ligand binding signal from the extracellular ligand-binding domain to the G protein-coupling 7-transmembrane domain2. In this manuscript, we propose a model for a sequential, multistep activation mechanism of metabotropic glutamate receptor subtype 5. We present a series of structures in lipid nanodiscs, from inactive to fully active, including agonist-bound intermediate states. Further, using bulk and single-molecule fluorescence imaging, we reveal distinct receptor conformations upon allosteric modulator and G protein binding.We propose a model for a sequential, multistep activation mechanism of metabotropic glutamate receptor subtype 5, including a series of structures in lipid nanodiscs, from inactive to fully active, with agonist-bound intermediate states. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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