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Tetrameric bacterial sodium channels: characterization of structure, stability, and drug binding

Nurani, G. and Radford, M. and O’Reilly, Andrias O. and Cronin, Nora and Haque, S. and Wallace, Bonnie A. (2008) Tetrameric bacterial sodium channels: characterization of structure, stability, and drug binding. Biochemistry 47 (31), pp. 8114-8121. ISSN 0006-2960.

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Official URL: http://dx.doi.org/10.1021/bi800645w

Abstract

NaChBac from Bacillus halodurans is a bacterial homologue of mammalian voltage-gated sodium channels. It has been proposed that a NaChBac monomer corresponds to a single domain of the mammalian sodium channel and that, like potassium channels, four monomers form a tetrameric channel. However, to date, although NaChBac has been well-characterized for functional properties by electrophysiological measurements on protein expressed in tissue culture, little information about its structural properties exists because of the difficulties in expressing the protein in large quantities. In this study, we present studies on the overexpression of NaChBac in Escherichia coli, purification of the functional detergent-solubilized channel, its identification as a tetramer, and characterization of its secondary structure, drug binding, and thermal stability. These studies are correlated with a model produced for the protein and provide new insights into the structure−function relationships of this sodium channel.

Item Type: Article
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 04 Aug 2010 14:09
Last Modified: 17 Apr 2013 12:17
URI: http://eprints.bbk.ac.uk/id/eprint/1193

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