{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Huang W"],"funding":["Agence Nationale de la Recherche (French National Research Agency)"],"pagination":["10345"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11604941"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["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 "],"journal":["Nature communications"],"pubmed_title":["Structural basis of orientated asymmetry in a mGlu heterodimer."],"pmcid":["PMC11604941"],"funding_grant_id":["ANR-10-INBS-04","ANR 18-CE11-0004-01"],"pubmed_authors":["Liu J","Qin J","Bonhomme L","Xu C","Shen C","Liu YR","Pin JP","Guo J","Xi K","Huang W","Zhang Y","Gao Y","Jin N","Quast RB","Margeat E","Shen DD","Rondard P","Song Y"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of orientated asymmetry in a mGlu heterodimer.","description":"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 ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-06-03T01:04:25.296Z","creation":"2025-04-04T01:58:22.293Z"},"accession":"S-EPMC11604941","cross_references":{"pubmed":["39609406"],"doi":["10.1038/s41467-024-54744-7"]}}