The binding site for GABA in the GABAaR is approximately 40 Angstroms from the gate of the ion channel. Much progress has been made in identifying the interactions that mediate the transfer of binding energy to cause opening of the channel gate. A critical discontinuity in the transfer of binding energy is at the interface of the ligand-binding and the transmembrane domains. Here the ligand binding energy is transmitted from beta strands in an immunoglobulin fold through loops connecting  those beta strands to alpha helices that ultimately must move to allow ion transport. Here we examine the electrostatic interactions that allow efficient transmission of that binding energy.

Electrostatic interaction at the interface of the ligand-binding and transmembrane  domains in the GABAa receptor

243rd National Meeting (2012)

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