Data from: Common internal allosteric network links anesthetic binding sites in a pentameric ligand-gated ion channel

General anesthetics bind reversibly to ion channels, modifying their
global conformational distributions, but the underlying atomic mechanisms
are not completely known. We examine this issue by way of the model
protein Gloeobacter violaceous ligand-gated ion channel (GLIC) using
computational molecular dynamics, with a coarse-grained model to enhance
sampling. We find that in flooding simulations, both propofol and a
generic particle localize to the crystallographic transmembrane anesthetic
binding region, and that propofol also localizes to an extracellular
region shared with the crystallographic ketamine binding site. Subsequent
simulations to probe these binding modes in greater detail demonstrate
that ligand binding induces structural asymmetry in GLIC. Consequently, we
employ residue interaction correlation analysis to describe the internal
allosteric network underlying the coupling of ligand and distant effector
sites necessary for conformational change. Overall, the results suggest
that the same allosteric network may underlie the actions of various
anesthetics, regardless of binding site.