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Updated: Aug 10, 2026

Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking
Published on: March 28, 2014
Pharmacological study on recombinant human GABA-A receptor complex containing alpha5 (leucine155 to valine) combined
1Department of Pharmacognosy, Beijing University of Traditional Chinese Medicine, Beijing 100029, China. Wangxiukun@263.net
Aim:
To investigate the characterization of the pharmacology of recombinant human GABA-A receptor complex containing alpha5beta3gamma2s subunits, and clarify which amino acids are essential for binding affinity.
Methods:
We constructed chimeric subunit of alpha5 (leucine mutated to valine in 155) by site-directed mutation, combined alpha5 or alpha5 (valine 155) with beta3gamma2s subunits by using the baculovirus-transfected Sf-9 insect cell expressing system. Fifteen commercially available effective compounds for the GABA binding recognition site were determined.
Results:
We found that competitive antagonist SR95531 and inhibitor Thio-4-piol increased IC50 values about 3 folds in alpha5 (valine155) beta3gamma2s compare to alpha5 (leucine155) beta3gamma2s receptor subunit combinations; Other GABA-A receptor ligands have little difference.
Conclusion:
The amino acid residues in 155 is important for the binding affinity and efficacy of SR95531 and Thio-4-piol to GABA-A receptor combinations containing an alpha5 subunit.
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