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Structure paper

TitleG protein selectivity in group I metabotropic glutamate receptors.
Journal, issue, pagesSci Adv, Vol. 12, Issue 28, Page eaee0044, Year 2026
Publish dateJul 10, 2026
AuthorsYue Lu / Tianlei Wen / Xuhang Lu / Guimin Zhang / Tingting Meng / Tianjin Liu / Xinyan Wang / Yuequan Shen / Xue Yang /
PubMed AbstractMetabotropic glutamate (mGlu) receptors are class C G protein-coupled receptor involved in synaptic transmission and neurological disorders. Group I mGlu receptors (mGlu1 and mGlu5) predominantly ...Metabotropic glutamate (mGlu) receptors are class C G protein-coupled receptor involved in synaptic transmission and neurological disorders. Group I mGlu receptors (mGlu1 and mGlu5) predominantly couple to G, whereas group II and III receptors primarily engage G. Although G-coupling mechanisms have been defined for several group II/III receptors, how group I receptors preferentially engage G remains unclear. Here we report cryo-electron microscopy structures of active mGlu-G protein complexes (mGlu1-G, mGlu1-G, mGlu5-G, and mGlu5-G) bound to l-glutamate and positive allosteric modulators (PAMs), together with two additional activated-state structures of mGlu1. Comparative structural and biochemical analyses identify a group I-specific ICL2 insertion that promotes preferential G engagement. Each receptor dimer asymmetrically binds one G protein heterotrimer via an intracellular pocket engaging the Gα amino-terminal helix. PAM binding to one 7TM domain induces W rotation and TM6 outward movement, bringing the two 7TMs into closer. These findings provide a structural basis for preferential G engagement and activation of group I mGlu receptors.
External linksSci Adv / PubMed:42430471 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 3.8 Å
Structure data

66174

9wqk

EMDB-66174, PDB-9wqk:
GRM5-Gi Complex Structure
Method: EM (single particle) / Resolution: 3.7 Å

66175

9wql

EMDB-66175, PDB-9wql:
GRM5-Gq Complex Structure
Method: EM (single particle) / Resolution: 3.2 Å

66176

9wqm

EMDB-66176, PDB-9wqm:
GRM1-Gi Complex Structure
Method: EM (single particle) / Resolution: 3.3 Å

66177

9wqn

EMDB-66177, PDB-9wqn:
GRM1-Gq Complex Structure
Method: EM (single particle) / Resolution: 3.7 Å

66178

9wqo

EMDB-66178, PDB-9wqo:
GRM1-Acc State Conformation 1
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-67294: GRM1-Gi Complex structure (focused refinement map 1)
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-67295: GRM1-Gi complex structure (focused refinement map 2)
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-67297: GRM1-Gq Complex Structure (Focused refinement map 2)
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-67298: GRM1-Gq Complex Structure (Focused refinement map 1)
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-67299: GRM1-Gq Complex (consensus map)
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-67317: GRM1-Acc State Conformation 2 (Consensus Map)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-67322: GRM1-Acc State Conformation 2 (Focused Refinement Map3)
Method: EM (single particle) / Resolution: 3.8 Å

81411

27tm

EMDB-81411, PDB-27tm:
GRM1-Acc State Conformation 2
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-GGL:
GAMMA-L-GLUTAMIC ACID

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CL:
Unknown entry

ChemComp-CLR:
CHOLESTEROL

PDB-1ex5:
FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE

ChemComp-YKU:
3-cyano-N-(1,3-diphenyl-1H-pyrazol-5-yl)benzamide / antipsychotic*YM

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / Receptor / Receptor complex

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