A structural determinant of desensitization and allosteric regulation by pentobarbitone of the GABAA receptor.

Birnir, Bryndis (author): John Curtin School of Medical Research, Australian National University

Tierney, M L (author)

Dalziel, J E (author)

Cox, G B (author)

Gage, P W (author)

(creator_code:org_t)

1997
1997
English.
In: Journal of Membrane Biology. - 0022-2631 .- 1432-1424. ; 155:2, s. 157-66

Abstract Subject headings

Functional properties of the alpha1beta1 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 beta1 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 beta1 subunit. The Hill coefficient of the peak current response to GABA was reduced to less than one also in a beta1 subunit-specific manner. It was concluded that the beta1 subunit dominated conformational changes activated by GABA.

By the author/editor: Birnir, Bryndis; Tierney, M L; Dalziel, J E; Cox, G B; Gage, P W

About the subject

MEDICAL AND HEALTH SCIENCES: MEDICAL AND HEAL ...; and Basic Medicine; and Physiology

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