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Structure paper

TitleG-protein activation by a metabotropic glutamate receptor.
Journal, issue, pagesNature, Vol. 595, Issue 7867, Page 450-454, Year 2021
Publish dateJun 30, 2021
AuthorsAlpay B Seven / Ximena Barros-Álvarez / Marine de Lapeyrière / Makaía M Papasergi-Scott / Michael J Robertson / Chensong Zhang / Robert M Nwokonko / Yang Gao / Justin G Meyerowitz / Jean-Philippe Rocher / Dominik Schelshorn / Brian K Kobilka / Jesper M Mathiesen / Georgios Skiniotis /
PubMed AbstractFamily 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 ...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. 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. Upon activation of the extracellular domain, the two transmembrane domains undergo extensive rearrangement in relative orientation to establish an asymmetric TM6-TM6 interface that promotes conformational changes in the cytoplasmic domain of one protomer. Nucleotide-bound G can be observed pre-coupled to inactive mGlu2, but its transition to the nucleotide-free form seems to depend on establishing the active-state TM6-TM6 interface. In contrast to family A and B GPCRs, G-protein coupling does not involve the cytoplasmic opening of TM6 but is facilitated through the coordination of intracellular loops 2 and 3, as well as a critical contribution from the C terminus of the receptor. The findings highlight the synergy of global and local conformational transitions to facilitate a new mode of G-protein activation.
External linksNature / PubMed:34194039 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.65 Å
Structure data

23994

7mtq

EMDB-23994, PDB-7mtq:
CryoEM Structure of Full-Length mGlu2 in Inactive-State Bound to Antagonist LY341495
Method: EM (single particle) / Resolution: 3.65 Å

23995

7mtr

EMDB-23995, PDB-7mtr:
CryoEM Structure of Full-Length mGlu2 Bound to Ago-PAM ADX55164 and Glutamate
Method: EM (single particle) / Resolution: 3.3 Å

23996

7mts

EMDB-23996, PDB-7mts:
CryoEM Structure of mGlu2 - Gi Complex
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-Z99:
2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine / antidepressant, antagonist*YM / LY-341495

ChemComp-GLU:
GLUTAMIC ACID / Glutamic acid

ChemComp-ZQY:
2-methoxy-6-propyl-N-(2-{4-[(1H-tetrazol-5-yl)methoxy]phenyl}ethyl)thieno[2,3-d]pyrimidin-4-amine

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN/ANTAGONIST / Metabotropic Glutamate Receptor 2 (mGlu2) (mGluR2) / Family C G protein-coupled receptor (GPCR) / Heterotrimeric G protein / CryoEM structure / MEMBRANE PROTEIN / MEMBRANE PROTEIN-ANTAGONIST complex / MEMBRANE PROTEIN/AGONIST / MEMBRANE PROTEIN-AGONIST complex / MEMBRANE PROTEIN/SIGNALING PROTEIN / MEMBRANE PROTEIN-SIGNALING PROTEIN complex

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