Amino acids lining the channel of the gamma-aminobutyric acid type A receptor identified by cysteine substitution.

@article{Xu1993AminoAL,
  title={Amino acids lining the channel of the gamma-aminobutyric acid type A receptor identified by cysteine substitution.},
  author={Mingzhi Xu and Myles H. Akabas},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 29},
  pages={21505-8}
}
The binding of gamma-aminobutyric acid (GABA) to gamma-aminobutyric acid type A (GABAA) receptors triggers the opening of an anion-selective channel. To identify amino acid residues that line the channel, we combined cysteine mutagenesis and covalent chemical modification. We mutated, one at a time, four consecutive residues (268-271) in the M2 membrane-spanning segment of the rat GABAA receptor alpha 1 subunit to cysteine and expressed the mutant alpha 1 subunits, together with either the beta… CONTINUE READING

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