Interpreting the impact of GABA_A receptor structural modifications using an allosteric co-agonist mechanism for etomidate actions

摘要

GABA_A receptors containing beta1 subunits are less sensitive to etomidate than those containing (J2, but whether this insensitivity is due to weak etomidate binding or low efficacy is uncertain. We utilized oocyte electrophysiology on both wild-type and gating mutant GABA_A receptors and estimated both binding and efficacy factors for etomidate based on an allosteric co-agonist mechanism. Our results suggest that fil subunits reduce etomidate efficacy, which is also interpreted as binding affinity in the open (active) state.