NDLI: The Fast Gating Mechanism in ClC-0 Channels

Content Provider	PubMed Central
Author	Bisset, David Corry, Ben Chung, Shin-ho
Copyright Year	2005
Abstract	We investigate and then modify the hypothesis that a glutamate side chain acts as the fast gate in ClC-0 channels. We first create a putative open-state configuration of the prokaryotic ClC Cl− channel using its crystallographic structure as a basis. Then, retaining the same pore shape, the prokaryotic ClC channel is converted to ClC-0 by replacing all the nonconserved polar and charged residues. Using this open-state channel model, we carry out molecular dynamics simulations to study how the glutamate side chain can move between open and closed configurations. When the side chain extends toward the extracellular end of the channel, it presents an electrostatic barrier to Cl− conduction. However, external Cl− ions can push the side chain into a more central position where, pressed against the channel wall, it does not impede the motion of Cl− ions. Additionally, a proton from a low-pH external solution can neutralize the extended glutamate side chain, which also removes the barrier to conduction. Finally, we use Brownian dynamics simulations to demonstrate the influence of membrane potential and external Cl− concentration on channel open probability.
Related Links	http://dx.doi.org/10.1529/biophysj.104.053447
Ending Page	186
Page Count	8
Starting Page	179
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	1
Volume Number	89
Language	English
Publisher	Biophysical Society
Publisher Date	2005-07-01
Access Restriction	Open
Rights Holder	Biophysical Society
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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