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Structure paper

TitleStructural basis of orientated asymmetry in a mGlu heterodimer.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 10345, Year 2024
Publish dateNov 28, 2024
AuthorsWeizhu Huang / Nan Jin / Jia Guo / Cangsong Shen / Chanjuan Xu / Kun Xi / Léo Bonhomme / Robert B Quast / Dan-Dan Shen / Jiao Qin / Yi-Ru Liu / Yuxuan Song / Yang Gao / Emmanuel Margeat / Philippe Rondard / Jean-Philippe Pin / Yan Zhang / Jianfeng Liu /
PubMed AbstractThe structural basis for the allosteric interactions within G protein-coupled receptors (GPCRs) heterodimers remains largely unknown. The metabotropic glutamate (mGlu) receptors are complex dimeric ...The structural basis for the allosteric interactions within G protein-coupled receptors (GPCRs) heterodimers remains largely unknown. The metabotropic glutamate (mGlu) receptors are complex dimeric GPCRs important for the fine tuning of many synapses. Heterodimeric mGlu receptors with specific allosteric properties have been identified in the brain. Here we report four cryo-electron microscopy structures of mGlu2-4 heterodimer in different states: an inactive state bound to antagonists, two intermediate states bound to either mGlu2 or mGlu4 agonist only and an active state bound to both glutamate and a mGlu4 positive allosteric modulator (PAM) in complex with Gi protein. In addition to revealing a unique PAM binding pocket among mGlu receptors, our data bring important information for the asymmetric activation of mGlu heterodimers. First, we show that agonist binding to a single subunit in the extracellular domain is not sufficient to stabilize an active dimer conformation. Single-molecule FRET data show that the monoliganded mGlu2-4 can be found in both intermediate states and an active one. Second, we provide a detailed view of the asymmetric interface in seven-transmembrane (7TM) domains and identified key residues within the mGlu2 7TM that limits its activation leaving mGlu4 as the only subunit activating G proteins.
External linksNat Commun / PubMed:39609406 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 5.95 Å
Structure data

37507

8wgb

EMDB-37507, PDB-8wgb:
mGlu2-4 heterodimer bound with Gi
Method: EM (single particle) / Resolution: 3.7 Å

37508

8wgc

EMDB-37508, PDB-8wgc:
heterodimer of mGlu2 and mGlu4 bound with mGlu2 agonist LY379268
Method: EM (single particle) / Resolution: 5.95 Å

EMDB-61789: mGlu2-4 heterodimer bound with Gi
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-61801: Cryo-EM structure of mGlu2-mGlu4 bound mGlu2 agonist LY379268
Method: EM (single particle) / Resolution: 5.95 Å

EMDB-61802: Cryo-EM structure of mGlu2-mGlu4 bound mGlu2 agonist LY379268
Method: EM (single particle) / Resolution: 3.78 Å

EMDB-61803: Cryo-EM structure of mGlu2-mGlu4 heterodimer bound with Gi
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-61804: Cryo-EM focused refined map of mGlu2-mGlu4 heterodimer bound with Gi
Method: EM (single particle) / Resolution: 3.49 Å

EMDB-61805: Cryo-EM focused refined map of mGlu2-mGlu4 heterodimer bound with Gi
Method: EM (single particle) / Resolution: 3.75 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID


ChemComp, No image

ChemComp-W9R:
Unknown entry


ChemComp, No image

ChemComp-W92:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / GPCR

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