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Article

Transmembrane domain 8 of the {gamma}-aminobutyric acid transporter GAT-1 lines a cytoplasmic accessibility pathway into its binding pocket.

The Journal of biological chemistry - 10 Apr 2009

Ben-Yona Assaf, Kanner Baruch I

Abstract excerpt

GAT-1 is a sodium- and chloride-coupled gamma-aminobutyric acid (GABA) transporter, which fulfills an essential role in the synaptic transmission by this neurotransmitter. Cysteine-399 is the major site of inhibition of GAT-1 by membrane-permeant sulfhydryl reagents. This cysteine residue was previously thought to reside on a cytoplasmic loop connecting transmembrane domains (TMs) 8 and 9. However, the crystal...

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Identifiers

PMID: 19201752
DOI: 10.1074/jbc.M809423200
PMCID: PMC2665093

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