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Voltage dependent membrane channels are formed by the zervamicins, a group of alpha-aminoisobutyric acid containing peptides. The role of polar residues like Thr, Gln and Hyp in promoting helical bundle formation is established by dramatically reduced channel lifetimes for a synthetic apolar analog. Crystal structures of Leu1-zervamicin reveal association of bent helices. Polar contacts between convex faces result in an 'hour glass' like arrangement of an aqueous channel with a central constriction. The structure suggests that gating mechanisms may involve movement of the Gln11 carboxamide group. Gln3 may play a role in modulating the size of the channel mouth.


Journal article


Biochem Biophys Res Commun

Publication Date





8 - 15


Amino Acid Sequence, Anti-Bacterial Agents, Electric Conductivity, Ion Channels, Lipid Bilayers, Models, Biological, Models, Molecular, Molecular Sequence Data, Peptaibols, Peptides, Phosphatidylcholines, Protein Conformation