The alpha5(H105R) mutation impairs alpha5 selective binding properties by altered positioning of the alpha5 subunit in GABAA receptors containing two distinct types of alpha subunits.

Abstract excerpt

GABA(A) receptors are pentameric ligand-gated ion channels that are major mediators of fast inhibitory neurotransmission. Clinically relevant GABA(A) receptor subtypes are assembled from alpha5(1-3, 5), beta1-3 and the gamma2 subunit. They exhibit a stoichiometry of two alpha, two beta and one gamma subunit, with two GABA binding sites located at the alpha/beta and one benzodiazepine binding site located at the...

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