Functional correlations of c-tail conformation in a skeletal muscle chloride channel /
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(Published version)
Date
2009
Authors
Ma, Linlin,
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thesis
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Abstract
Like other CLC channel and transporter proteins, hClC-1 is homodimeric with a separate chloride permeation pore in each subunit. It has two distinct gating processes, fast gating which regulates each pore independently and common gating which closes both pores simultaneously. Fast gating is associated with a glutamate side-chain carboxyl group that swings into and out of each permeation pathway, although some evidence suggests that changes in pore conformation might also be involved. Common gating, however, is much more complicated and remains poorly understood. The objectives, therefore, were to investigate the common gating of hClC-1, especially unknown aspects of the conformation of its long cytoplasmic carboxyl-tail (C-tail) and interactions between its C-tail and membrane-resident regions. Anticipating the C-tail‘s two cystathionine beta-synthase (CBS) domains might be functionally important, the project used mutagenesis, split channel methods, GST-pulldown and patch-clamping to assess suspected contact between them. Strong binding of a membrane-resident channel fragment, N720 (M1 to S720) containing CBS1, to its complement was found, 721C (G721 to L988) containing CBS2.
School/Discipline
University of South Australia. School of Pharmacy and Medical Sciences.
School of Pharmacy and Medical Sciences
School of Pharmacy and Medical Sciences
Dissertation Note
Thesis (PhD)--University of South Australia, 2009.
Provenance
Copyright 2009 Linlin Ma. This work is made available under the Creative Commons Attribution-NonCommercial-NoDerivs Australia 3.0 licence (http://creativecommons.org/licenses/by-nc-nd/3.0/au/)
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1 volume (various pagings) :
illustrations (some colour).
Includes bibliographical references.
illustrations (some colour).
Includes bibliographical references.
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