Article
Agonist-specific conformational changes in the α1-γ2 subunit interface of the GABA A receptor.
Molecular pharmacology - 1 Aug 2012
Eaton Megan M, Lim You Bin, Bracamontes John, Steinbach Joe Henry, Akk Gustav
Abstract excerpt
The GABA(A) receptor undergoes conformational changes upon the binding of agonist that lead to the opening of the channel gate and a flow of small anions across the cell membrane. Besides the transmitter GABA, allosteric ligands such as the general anesthetics pentobarbital and etomidate can activate the receptor. Here, we have investigated the agonist specificity of structural changes in the extracellular domain...
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