Theoretical studies of the M2 transmembrane segment of the glycine receptor: models of the open pore structure and current-voltage characteristics.

ABSTRACT: The pentameric glycine receptor (GlyR), a member of the nicotinicoid superfamily of ligand-gated ion channels, is an inhibitory Cl(-) channel that is gated by glycine. Using recently published NMR data of the second transmembrane segment (M2) of the human alpha1 GlyR, structural models of pentameric assemblies embedded in a lipid bilayer were constructed using a combination of experimentally determined constraints coupled with all-atom energy minimization. Based on this structure of the pentameric M2 "pore", Brownian dynamics simulations of ion permeation through this putative conducting open state of the channel were carried out. Simulated I-V curves were in good agreement with published experimental current-voltage curves and the anion/cation permeability ratio, suggesting that our open-

SUBMITTER: Cheng MH 

PROVIDER: S-EPMC1366671 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature