The βN265M mutation reduces the channel gating effects of a α1M236W mutation that mimics etomidate.

<p><b>Panel A)</b> Data are reproduced from Guitchounts et al <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0111470#pone.0111470-Guitchounts1" target="_blank">[38]</a> showing mean ± SD GABA concentration-response, normalized to maximal currents, from oocytes expressing concatenated receptor dimer and trimer constructs. Lines through data points represent non-linear least squares logistic fits (Eq. 1, methods). Solid squares represent β2-α1/γ2L-β2-α1 receptors (GABA EC₅₀ = 36 µM) and open circles represent β2-α1M236W/γ2L-β2-α1M236W receptors (EC₅₀ = 1.0 µM). <b>Panel</b> <b>B)</b> Data points are mean ± SD current responses to GABA, normalized to maximal currents. Solid diamonds represent β2N265M-α1/γ2L-β2N265M-α1 receptors (GABA EC₅₀ = 76 µM; 95% CI = 63 to 92 µM) and open triangles represent β2N265M-α1M236W/γ2L-β2N265M-α1M236W- receptors (EC₅₀ = 25 µM; 95% CI = 22 to 29 µM).