Article
Probing the pharmacological properties of distinct subunit interfaces within heteromeric glycine receptors reveals a functional ββ agonist-binding site.
Journal of neurochemistry - 1 Jul 2012
Dutertre Sébastien, Drwal Malgorzata, Laube Bodo, Betz Heinrich
Abstract excerpt
Synaptic glycine receptors (GlyRs) are hetero-pentameric chloride channels composed of α and β subunits, which are activated by agonist binding at subunit interfaces. To examine the pharmacological properties of each potential agonist-binding site, we substituted residues of the GlyR α(1) subunit by the corresponding residues of the β subunit, as deduced from sequence alignment and homology modeling based on the...
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- Computer Simulation
- Copper
- Ethanol
- Glycine Agents
- Inhibitory Concentration 50
- Ivermectin
- Membrane Potentials
- Microinjections