Two tyrosine residues on the alpha subunit are crucial for benzodiazepine binding and allosteric modulation of gamma-aminobutyric acidA receptors.

@article{Amin1997TwoTR,
  title={Two tyrosine residues on the alpha subunit are crucial for benzodiazepine binding and allosteric modulation of gamma-aminobutyric acidA receptors.},
  author={Jahanshah Amin and Amy R Brooks-Kayal and David S Weiss},
  journal={Molecular pharmacology},
  year={1997},
  volume={51 5},
  pages={833-41}
}
Benzodiazepines (BZs) exert their therapeutic effects in the mammalian central nervous system at least in part by modulating the activation of gamma-aminobutyric acid (GABA)-activated chloride channels. To gain further insight into the mechanism of action of BZs on GABA receptors, we have been investigating structural determinants required for the actions of the BZ diazepam (dzp) on recombinant alpha1 beta2 gamma2 GABA(A) receptors. Site-directed mutagenesis was used to introduce point… CONTINUE READING

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