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Binding of Inhalational Anesthetics to the Transmembrane Domain of the Human g‐aminobutyric acid Aa1 (GABAAa1) Receptor.
Author(s) -
Manderson Gavin Andrew,
Johansson Jonas S
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a96
Subject(s) - aminobutyric acid , transmembrane domain , chemistry , transmembrane protein , receptor , fusion protein , biophysics , gabaa receptor , biochemistry , recombinant dna , biology , gene
Currently, it is thought that inhalational anesthetics cause anesthesia by binding amongst the four α‐helices of the transmembrane domain of ligand‐gated ion channels, such as the γ‐aminobutyric acid A (GABA A receptor. To investigate this, we have expressed the transmembrane domain of the human γ‐aminobutyric acid Aα1 (GABA A α 1 ) receptor as a glutathione‐s‐transferase (GST) fusion protein. Because of the hydrophobic nature of the GABA portion, all physicochemical characterizations and anesthetic binding measurements are being made using the intact fusion construct. Data are then compared with those collected for the “blank” GST, expressed and purified under the same conditions as the full‐length construct. Supported by NIH GM65218.