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TitleAgonists and allosteric modulators promote signaling from different metabotropic glutamate receptor 5 conformations.
Journal, issue, pagesCell Rep, Vol. 36, Issue 9, Page 109648, Year 2021
Publish dateAug 31, 2021
AuthorsChady Nasrallah / Giuseppe Cannone / Julie Briot / Karine Rottier / Alice E Berizzi / Chia-Ying Huang / Robert B Quast / Francois Hoh / Jean-Louis Banères / Fanny Malhaire / Ludovic Berto / Anaëlle Dumazer / Joan Font-Ingles / Xavier Gómez-Santacana / Juanlo Catena / Julie Kniazeff / Cyril Goudet / Amadeu Llebaria / Jean-Philippe Pin / Kutti R Vinothkumar / Guillaume Lebon /
PubMed AbstractMetabotropic glutamate receptors (mGluRs) are dimeric G-protein-coupled receptors activated by the main excitatory neurotransmitter, L-glutamate. mGluR activation by agonists binding in the venus ...Metabotropic glutamate receptors (mGluRs) are dimeric G-protein-coupled receptors activated by the main excitatory neurotransmitter, L-glutamate. mGluR activation by agonists binding in the venus flytrap domain is regulated by positive (PAM) or negative (NAM) allosteric modulators binding to the 7-transmembrane domain (7TM). We report the cryo-electron microscopy structures of fully inactive and intermediate-active conformations of mGlu receptor bound to an antagonist and a NAM or an agonist and a PAM, respectively, as well as the crystal structure of the 7TM bound to a photoswitchable NAM. The agonist induces a large movement between the subunits, bringing the 7TMs together and stabilizing a 7TM conformation structurally similar to the inactive state. Using functional approaches, we demonstrate that the PAM stabilizes a 7TM active conformation independent of the conformational changes induced by agonists, representing an alternative mode of mGlu activation. These findings provide a structural basis for different mGluR activation modes.
External linksCell Rep / PubMed:34469715 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.54 - 4.0 Å
Structure data

31536

7fd8

EMDB-31536, PDB-7fd8:
Thermostabilised full length human mGluR5-5M bound with L-quisqualic acid
Method: EM (single particle) / Resolution: 3.8 Å

31537

7fd9

EMDB-31537, PDB-7fd9:
Thermostabilised full length human mGluR5-5M with orthosteric antagonist, LY341495
Method: EM (single particle) / Resolution: 4.0 Å

PDB-7p2l:
thermostabilised 7TM domain of human mGlu5 receptor bound to photoswitchable ligand alloswitch-1
Method: X-RAY DIFFRACTION / Resolution: 2.54 Å

Chemicals

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

ChemComp-QUS:
(S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID / agonist*YM / Quisqualic acid

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

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

ChemComp-4YI:
2-chloranyl-~{N}-[2-methoxy-4-[(~{E})-pyridin-2-yldiazenyl]phenyl]benzamide

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • enterobacteria phage t4 (virus)
KeywordsMEMBRANE PROTEIN / G protein coupled receptors / Signal transduction / Metabotropic glutamate receptor 5 (GRM5) / G-protein coupled receptors / metabotropic glutamate receptor / inactive state / SIGNALING PROTEIN / G protein coupled receptor / mGlu5 7TM / photoswitchable ligand / allosteric modulator

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