ArticleBiophysical journal2005
The fast gating mechanism in ClC-0 channels.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 35 citations in OpenAlex.
- Dynamical model of the CLC-2 ion channel reveals conformational changes associated with selectivity-filter gating.PLoS computational biology · 2020Article
- Chloride Ion Transport by theFrontiers in chemistry · 2018Article
- Two Cl Ions and a Glu Compete for a Helix Cage in the CLC Proton/ClBiophysical journal · 2017Article
- Probing the conformation of a conserved glutamic acid within the ClThe Journal of general physiology · 2017Article
- A tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes.The Journal of physiology · 2015Review
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- Sequential interaction of chloride and proton ions with the fast gate steer the voltage-dependent gating in ClC-2 chloride channels.The Journal of physiology · 2012Article
- Influences of mutations on the electrostatic binding free energies of chloride ions in Escherichia coli ClC.The journal of physical chemistry. B · 2012Article
- A three-state multi-ion kinetic model for conduction properties of ClC-0 chloride channel.Biophysical journal · 2010Article
- Secondary water pore formation for proton transport in a ClC exchanger revealed by an atomistic molecular-dynamics simulation.Biophysical journal · 2010Article
- Intracellular proton regulation of ClC-0.The Journal of general physiology · 2008Article
- The mechanism of fast-gate opening in ClC-0.The Journal of general physiology · 2007Article
- Carboxy terminus splice variation alters ClC channel gating and extracellular cysteine reactivity.Biophysical journal · 2006Article
- Proton sensing of CLC-0 mutant E166D.The Journal of general physiology · 2006Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.