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Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains

Zubcevic, L and Bavro, VN and Muniz, JRC and Schmidt, MR and Wang, S and De Zorzi, R and Venien-Bryan, C and Sansom, MSP and Nichols, CG and Tucker, SJ (2014) 'Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.' Journal of Biological Chemistry, 289 (1). 143 - 151. ISSN 0021-9258

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Abstract

KirBac channels are prokaryotic homologs of mammalian inwardly rectifying potassium (Kir) channels, and recent structures of KirBac3.1 have provided important insights into the structural basis of gating in Kir channels. In this study, we demonstrate that KirBac3.1 channel activity is strongly pH-dependent, and we used x-ray crystallography to determine the structural changes that arise from an activatory mutation (S205L) located in the cytoplasmic domain (CTD). This mutation stabilizes a novel energetically favorable open conformation in which changes at the intersubunit interface in the CTD also alter the electrostatic potential of the inner cytoplasmic cavity. These results provide a structural explanation for the activatory effect of this mutation and provide a greater insight into the role of the CTD in Kir channel gating. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 15 Dec 2016 14:13
Last Modified: 05 Feb 2019 18:15
URI: http://repository.essex.ac.uk/id/eprint/17731

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