Abstract
The point mutation H101R in the alpha1-subunit of gamma-aminobutyric acid type A receptors is known to abolish effects by benzodiazepine diazepam. This mutation and homologous mutations in other alpha-subunits have been used to quantify receptor pentamers containing two different alpha-subunit isoforms, and to study the role of alpha-subunit isoforms in the response of mice to diazepam. Both types of study assumed implicitly or explicitly that this mutation strongly affects assembly with the gamma2-subunit. Here, we investigated the assembly properties of mutated in comparison with wild-type subunits, and demonstrate that alpha1H101R has similar assembly properties as wild-type alpha1.
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