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Article

Conformationally sensitive proximity of extracellular loops 2 and 4 of the γ-aminobutyric acid (GABA) transporter GAT-1 inferred from paired cysteine mutagenesis.

The Journal of biological chemistry - 5 Dec 2014

Hilwi Maram, Dayan Oshrat, Kanner Baruch I

Abstract excerpt

The sodium- and chloride-coupled GABA transporter GAT-1 is a member of the neurotransmitter:sodium:symporters, which are crucial for synaptic transmission. Structural work on the bacterial homologue LeuT suggests that extracellular loop 4 closes the extracellular solvent pathway when the transporter becomes inward-facing. To test whether this model can be extrapolated to GAT-1, cysteine residues were introduced...

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Identifiers

PMID: 25339171
DOI: 10.1074/jbc.M114.593061
PMCID: PMC4256357

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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