Agarwalla, S and Mellor, IR and Sansom, MSP and Karle, IL and Flippen-Anderson, JL and Uma, K and Krishna, K and Sukumar, M and Balaram, P (1992) Zervamicins, a structurally characterised peptide model for membrane ion channels. In: Biochemical and Biophysical Research Communications, 186 (1). pp. 8-15.
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Voltage dependent membrane channels are formed by the zervamicins, a group of α-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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||19 May 2010 07:05|
|Last Modified:||19 Sep 2010 06:00|
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