CryoEM Structure of Full-Length mGlu2 Bound to Ago-PAM ADX55164 and Glutamate
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ABSTRACT:
SUBMITTER: Georgios Skiniotis
PROVIDER: EMPIAR-10978 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
G-protein activation by a metabotropic glutamate receptor.
Seven Alpay B AB Barros-Álvarez Ximena X de Lapeyrière Marine M Papasergi-Scott Makaía M MM Robertson Michael J MJ Zhang Chensong C Nwokonko Robert M RM Gao Yang Y Meyerowitz Justin G JG Rocher Jean-Philippe JP Schelshorn Dominik D Kobilka Brian K BK Mathiesen Jesper M JM Skiniotis Georgios G
Nature 20210630 7867
Family C G-protein-coupled receptors (GPCRs) operate as obligate dimers with extracellular domains that recognize small ligands, leading to G-protein activation on the transmembrane (TM) domains of these receptors by an unknown mechanism<sup>1</sup>. Here we show structures of homodimers of the family C metabotropic glutamate receptor 2 (mGlu2) in distinct functional states and in complex with heterotrimeric G<sub>i</sub>. Upon activation of the extracellular domain, the two transmembrane domain ...[more]
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