Daniel T. Infield, Ali Rasouli, Grace G. Galles, Christophe Chipot, Emad
Tajkhorshid, and Christopher A. Ahern.
Cation-π interactions and their functional roles in membrane
proteins.
Journal of Molecular Biology, 433:167035, 2021.
(PMC: PMC8338773)
INFI2021-ET
Membrane proteins rely on diverse molecular forces to execute
essential physiological tasks. Cation- interactions arise as a
result of strong attractive forces between positively charged
entities and the -electron cloud of aromatic groups. The
physicochemical characteristics of cation- interactions are
particularly well-suited to the dual hydrophobic/hydrophilic
environment of membrane proteins, and they have been shown to play
important roles in membrane protein function. As high-resolution
structural data of membrane proteins bring molecular features into
increasingly sharper view, cation- interactions are gaining
traction as essential contributors to membrane protein chemistry,
function, and pharmacology. Herein, after briefly reviewing the
physicochemical properties of cation- interactions, we present
several examples of prominent cation- interactions in ion
channels and other membrane proteins, and we highlight their specific
functional roles.
