Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels.

ABSTRACT: Pentameric ligand-gated ion channels are activated by the binding of agonists to a site distant from the ion conduction path. These membrane proteins consist of distinct ligand-binding and pore domains that interact via an extended interface. Here, we have investigated the role of residues at this interface for channel activation to define critical interactions that couple conformational changes between the two structural units. By characterizing point mutants of the prokaryotic channels ELIC and GLIC by electrophysiology, X-ray crystallography and isothermal titration calorimetry, we have identified conserved residues that, upon mutation, apparently prevent activation but not ligand binding. The positions of nonactivating mutants cluster at a loop within the extracellular domain connectin

SUBMITTER: Bertozzi C 

PROVIDER: S-EPMC4778918 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature