Dynamic closed states of a ligand-gated ion channel captured by cryo-EM and simulations.

ABSTRACT: Ligand-gated ion channels are critical mediators of electrochemical signal transduction across evolution. Biophysical and pharmacological characterization of these receptor proteins relies on high-quality structures in multiple, subtly distinct functional states. However, structural data in this family remain limited, particularly for resting and intermediate states on the activation pathway. Here, we report cryo-electron microscopy (cryo-EM) structures of the proton-activated Gloeobacter violaceus ligand-gated ion channel (GLIC) under three pH conditions. Decreased pH was associated with improved resolution and side chain rearrangements at the subunit/domain interface, particularly involving functionally important residues in the β1-β2 and M2-M3 loops. Molecular dynamics simulation

SUBMITTER: Rovsnik U 

PROVIDER: S-EPMC8326787 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature