Futaki S, Asami K.Ligand-induced extramembrane conformation
switch controlling alamethicin assembly and the channel current.
Chem Biodivers. 2007 Jun;4(6):1313-22.
Institute for Chemical Research, Kyoto University, Uji,
Kyoto, Japan.
futaki@scl.kyoto-u.ac.jp
In this review, we describe our approach to creating artificial
receptor-channel proteins or sensor systems, using an
extramembrane segment conformationally switchable by external
stimuli. Alamethicin is known to self-assemble in membranes to
form ion channels with various open states. Employment of an
alpha-helical leucine-zipper segment resulted in the effective
modulation of the association states of alamethicin to produce a
single predominant channel-open state. A decrease in the helical
content of the extramembrane segments was found to induce a
channel-current increase. Therefore, conformational changes in
the extramembrane segments induced by the interaction with
ligands can be reflected in the current levels.
PMID: 17589883
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