Correlating structural and energetic changes in glycine receptor activation.

ABSTRACT: Pentameric ligand-gated ion channels (pLGICs) mediate fast chemoelectrical transduction in the nervous system. The mechanism by which the energy of ligand binding leads to current-conducting receptors is poorly understood and may vary among family members. We addressed these questions by correlating the structural and energetic mechanisms by which a naturally occurring M1 domain mutation (α1(Q-26'E)) enhances receptor activation in homo- and heteromeric glycine receptors. We systematically altered the charge of spatially clustered residues at positions 19' and 24', in the M2 and M2-M3 linker domains, respectively, which are known to be critical to efficient receptor activation, on a background of α1(Q-26'E). Changes in the durations of single receptor activations (clusters) and conductance

SUBMITTER: Scott S 

PROVIDER: S-EPMC4342475 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature