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Structure paper

TitleDelta-type glutamate receptors are ligand-gated ion channels.
Journal, issue, pagesNature, Vol. 647, Issue 8091, Page 1063-1071, Year 2025
Publish dateSep 16, 2025
AuthorsHaobo Wang / Fairine Ahmed / Jeffrey Khau / Anish Kumar Mondal / Edward C Twomey /
PubMed AbstractDelta-type ionotropic glutamate receptors (iGluRs, also known as GluDs) are members of the iGluR ligand-gated ion channel family, yet their function remains unknown. Although GluDs are widely ...Delta-type ionotropic glutamate receptors (iGluRs, also known as GluDs) are members of the iGluR ligand-gated ion channel family, yet their function remains unknown. Although GluDs are widely expressed in the brain, have key roles in synaptic organization, and harbour disease-linked mutations, whether they retain iGluR-like channel function is debated as currents have not been directly observed. Here we define GluDs as ligand-gated ion channels that are tightly regulated in cellular contexts by purifying human GluD2 (hGluD2) and directly characterizing its structure and function using cryo-electron microscopy and bilayer recordings. We show that hGluD2 is activated by D-serine and GABA (γ-aminobutyric acid), with augmented activation at physiological temperatures. We reveal that hGluD2 contains an ion channel directly coupled to clamshell-like ligand-binding domains, which are coordinated by the amino-terminal domain above the ion channel. Ligand binding triggers channel opening via an asymmetric mechanism, and a cerebellar ataxia point mutation in the ligand-binding domain rearranges the receptor architecture and induces leak currents. Our findings demonstrate that GluDs possess the intrinsic biophysical properties of ligand-gated ion channels, reconciling prior conflicting observations to establish a framework for understanding their cellular regulation and for developing therapies targeting GluD2.
External linksNature / PubMed:40957579 / PubMed Central
MethodsEM (single particle)
Resolution3.57 - 3.74 Å
Structure data

49888

9nwo

EMDB-49888, PDB-9nwo:
Human delta 2 receptor in the resting state
Method: EM (single particle) / Resolution: 3.57 Å

49889

9nwp

EMDB-49889, PDB-9nwp:
Human delta 2 receptor activated by D-serine
Method: EM (single particle) / Resolution: 3.69 Å

49890

9nwq

EMDB-49890, PDB-9nwq:
Human delta 2 receptor in the resting state with ATD deleted
Method: EM (single particle) / Resolution: 3.74 Å

70667

9ooo

EMDB-70667, PDB-9ooo:
Human delta 2 receptor with R710W Cerebellar Ataxia mutation in the apo closed state
Method: EM (single particle) / Resolution: 3.68 Å

70668

9oop

EMDB-70668, PDB-9oop:
Human delta 2 receptor with R710W Cerebellar Ataxia mutation in the apo leak state
Method: EM (single particle) / Resolution: 3.73 Å

Chemicals

ChemComp-DSN:
D-SERINE

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Ligand-gated ion channel / ion channel / neurotransmitter receptor

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