A Structural Determinant of Desensitization and Allosteric Regulation by Pentobarbitone of the GABA A Receptor
| Autor: | Julie E. Dalziel, Bryndis Birnir, Graeme B. Cox, M L Tierney, Peter W. Gage |
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| Rok vydání: | 1997 |
| Předmět: |
Patch-Clamp Techniques
Physiology medicine.medical_treatment Protein subunit Molecular Sequence Data Allosteric regulation Biophysics Biology GABAA-rho receptor Allosteric Regulation Receptors GABA medicine Humans Amino Acid Sequence Threonine Pentobarbital gamma-Aminobutyric Acid Desensitization (medicine) Dose-Response Relationship Drug GABAA receptor Long-term potentiation Cell Biology Glutamine Biochemistry Mutagenesis Site-Directed Baculoviridae |
| Zdroj: | Journal of Membrane Biology. 155:157-166 |
| ISSN: | 1432-1424 0022-2631 |
| DOI: | 10.1007/s002329900167 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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