A Single M1 Residue in the β2 Subunit Alters Channel Gating of GABAA Receptor in Anesthetic Modulation and Direct Activation*

@article{Chang2003ASM,
  title={A Single M1 Residue in the $\beta$2 Subunit Alters Channel Gating of GABAA Receptor in Anesthetic Modulation and Direct Activation*},
  author={Chang-sheng S Chang and Riccardo Olcese and Richard W. Olsen},
  journal={Journal of Biological Chemistry},
  year={2003},
  volume={278},
  pages={42821 - 42828}
}
General anesthetics allosterically modulate the activity of neuronal γ-aminobutyric acid, type A (GABAA), receptors. Previous mutational studies from our laboratory and others have shown that the regions in transmembrane domain 1 (M1) and pre-M1 of α and β subunits in GABA receptors are essential for positive modulation of GABA binding and function by the intravenous (IV) general anesthetics. Mutation of β2Gly-219 to Phe corresponded in ρ nearly eliminated the modulatory effect of IV… Expand
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