Microsecond simulations indicate that ethanol binds between subunits and could stabilize an open-state model of a glycine receptor.

ABSTRACT: Cys-loop receptors constitute a superfamily of ion channels gated by ligands such as acetylcholine, serotonin, glycine, and γ-aminobutyric acid. All of these receptors are thought to share structural characteristics, but due to high sequence variation and limited structure availability, our knowledge about allosteric binding sites is still limited. These sites are frequent targets of anesthetic and alcohol molecules, and are of high pharmacological importance. We used molecular simulations to study ethanol binding and equilibrium exchange for the homomeric α1 glycine receptor (GlyRα1), modeled on the structure of the Gloeobacter violaceus pentameric ligand-gated channel. Ethanol has a well-known potentiating effect and can be used in high concentrations. By performing two microsecond-scale

SUBMITTER: Murail S 

PROVIDER: S-EPMC3072665 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature