A structural determinant of desensitization and allosteric regulation by pentobarbitone of the GABA(A) receptor

被引：47

作者：

Birnir, B ^{[1
]}

Tierney, ML ^{[1
]}

Dalziel, JE ^{[1
]}

Cox, GB ^{[1
]}

Gage, PW ^{[1
]}

机构：

[1] MRC,MOL BIOL LAB,CAMBRIDGE,ENGLAND

来源：

JOURNAL OF MEMBRANE BIOLOGY | 1997年 / 155卷 / 02期

关键词：

M2; baculovirus; expression; ligand gated; patch clamp; GABA(A) subunit;

D O I：

10.1007/s002329900167

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Functional properties of the alpha(1) beta(1) GABA(A) 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 beta(1) mutants. A negligible plateau current and abolition of potentiation by pentobarbitone of the GABA-activated current depended on the Thr 12' Gin mutation being present in the beta(1) subunit. The Hill coefficient of the peak current response to GABA was reduced to less than one also in a beta(1) subunit-specific manner. It was concluded that the beta(1) subunit dominated conformational changes activated by GABA.

引用

页码：157 / 166

页数：10

共 43 条

[1] GABA(A) RECEPTOR NEEDS 2 HOMOLOGOUS DOMAINS OF THE BETA-SUBUNIT FOR ACTIVATION BY GABA BUT NOT BY PENTOBARBITAL [J].