Functional evaluation of key interactions evident in the structure of the eukaryotic Cys-loop receptor GluCl.

ABSTRACT: The publication of the first high-resolution crystal structure of a eukaryotic Cys-loop receptor, GluClα, has provided valuable structural information on this important class of ligand-gated ion channels (LGIC). However, limited functional data exist for the GluCl receptors. Before applying the structural insights from GluCl to mammalian Cys-loop receptors such as nicotinic acetylcholine and GABA receptors, it is important to ensure that established functional features of mammalian Cys-loop receptors are present in the more distantly related GluCl receptors. Here, we seek to identify ligand-binding interactions that are generally associated with Cys-loop receptors, including the frequently observed cation-π interaction. Our studies were performed on the highly homologous GluClβ receptor, b

SUBMITTER: Daeffler KN 

PROVIDER: S-EPMC4201344 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature