Assessment of homology templates and an anesthetic binding site within the γ-aminobutyric acid receptor.

ABSTRACT:

Background

Anesthetics mediate portions of their activity via modulation of the γ-aminobutyric acid receptor (GABAaR). Although its molecular structure remains unknown, significant progress has been made toward understanding its interactions with anesthetics via molecular modeling.

Methods

The structure of the torpedo acetylcholine receptor (nAChRα), the structures of the α4 and β2 subunits of the human nAChR, the structures of the eukaryotic glutamate-gated chloride channel (GluCl), and the prokaryotic pH-sensing channels, from Gloeobacter violaceus and Erwinia chrysanthemi, were aligned with the SAlign and 3DMA algorithms. A multiple sequence alignment from these structures and those of the GABAaR was performed with ClustalW. The Modeler and Rosetta algorithms independentl

SUBMITTER: Bertaccini EJ 

PROVIDER: S-EPMC3823821 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature