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TitleStructural basis for selective inhibition of human GABA transporter GAT3.
Journal, issue, pagesNat Commun, Year 2026
Publish dateJan 29, 2026
AuthorsJonas Sigurd Mortensen / Francesco Bavo / Malene Hall Jensen / Alexander Peder Smiszek Pedersen / Julian Philipp Storm / Tillmann Pape / Bente Frølund / Petrine Wellendorph / Azadeh Shahsavar /
PubMed AbstractThe astrocytic γ-aminobutyric acid (GABA) transporter, GAT3, is essential for terminating GABAergic signaling in the central nervous system. Selective inhibition of GAT3 offers a potential strategy ...The astrocytic γ-aminobutyric acid (GABA) transporter, GAT3, is essential for terminating GABAergic signaling in the central nervous system. Selective inhibition of GAT3 offers a potential strategy for elevating extracellular GABA levels for the treatment of neurological disorders including epilepsy. However, few potent and selective GAT3 inhibitors have been developed, and their mechanisms of inhibition remain poorly understood. Here, we present the cryo-electron microscopy structures of full-length, wild-type human GAT3, hGAT3, bound to a selective inhibitor, to substrate GABA, or in substrate-free state. hGAT3 bound to the inhibitor or in the substrate-free state exhibits an inward-open conformation. The inhibitor binds within the intracellular permeation pathway, positioned between transmembrane helices 1, 2, 3, 6, 7, and 8. The GABA-bound hGAT3 is captured in an inward-occluded state, revealing the ion coordination and substrate recognition network, including a cation-π interaction between GABA's γ-amino group and a phenylalanine residue in transmembrane helix 6. Our data reveal the molecular determinants for the inhibitor selectivity, and the mode of substrate binding and transport inhibition, providing blueprints for the rational design of next-generation selective GAT3 inhibitors.
External linksNat Commun / PubMed:41611703
MethodsEM (single particle)
Resolution2.9 Å
Structure data

53259

9qo8

EMDB-53259, PDB-9qo8:
Inward-open structure of human GABA transporter 3 bound to selective inhibitor SR-THAP
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

PDB-1i87:
SOLUTION STRUCTURE OF THE WATER-SOLUBLE FRAGMENT OF RAT HEPATIC APOCYTOCHROME B5

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Transport protein / SLC6A11 / neurotransmitter/sodium symporter / Sodium- and chloride-dependent GABA transporter 3 / GAT3

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