Functional properties of the α1β1 GABAA receptor changes in a subunit-specific manner when a threonine residue in the M2 region at the 12′ position was mutated to glutamine. The rate and extent of desensitization increased in all mutants but the rate of activation was faster in the β1 mutants. A negligible plateau current and abolition of potentiation by pentobarbitone of the GABA-activated current depended on the Thr 12′ Gln mutation being present in the β1 subunit. The Hill coefficient of the peak current response to GABA was reduced to less than one also in a β1 subunit-specific manner. It was concluded that the β1 subunit dominated conformational changes activated by GABA.
The Journal of Membrane Biology – Springer Journals
Published: Jan 15, 1997
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