Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

Biochem Biophys Res Commun

Publication Date

15/07/1992

Volume

186

Pages

8 - 15

Keywords

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