Mutation of glycine receptor subunit creates beta-alanine receptor responsive to GABA.

@article{Schmieden1993MutationOG,
  title={Mutation of glycine receptor subunit creates beta-alanine receptor responsive to GABA.},
  author={Volker Schmieden and Jochen Kuhse and Heinrich Betz},
  journal={Science},
  year={1993},
  volume={262 5131},
  pages={256-8}
}
The amino acid at position 160 of the ligand-binding subunit, alpha 1, is an important determinant of agonist and antagonist binding to the glycine receptor. Exchange of the neighboring residues, phenylalanine at position 159 and tyrosine at position 161, increased the efficacy of amino acid agonists. Whereas wild-type alpha 1 channels expressed in Xenopus oocytes required 0.7 millimolar beta-alanine for a half-maximal response, the doubly mutated (F159Y,Y161F) alpha 1 subunit had an affinity… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 31 extracted citations

Defining affinity with the GABAA receptor.

The Journal of neuroscience : the official journal of the Society for Neuroscience • 1998
View 11 Excerpts
Highly Influenced

Molecular biology of the GABA(A) receptor: functional domains implicated by mutational analysis.

Frontiers in bioscience : a journal and virtual library • 1996
View 12 Excerpts
Highly Influenced

Molecular pharmacology of the glycine receptor chloride channel.

Current pharmaceutical design • 2007
View 6 Excerpts
Highly Influenced

Inhibitory glutamate receptor channels

Molecular Neurobiology • 1996
View 3 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…