ArticleBiophysical journal2007
The protonation state of the Glu-71/Asp-80 residues in the KcsA potassium channel: a first-principles QM/MM molecular dynamics study.
Article in Biophysical journal, 2007. 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.
- Fluoride Transport and Inhibition Across CLC Transporters.Handbook of experimental pharmacology · 2024Article
- Unraveling of a Strongly Correlated Dynamical Network of Residues Controlling the Permeation of Potassium in KcsA Ion Channel.Entropy (Basel, Switzerland) · 2021Article
- The influence of membrane bilayer thickness on KcsA channel activity.Channels (Austin, Tex.) · 2019Article
- Chloride Ion Transport by theFrontiers in chemistry · 2018Article
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- Protonation state of E71 in KcsA and its role for channel collapse and inactivation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Ion selectivity in channels and transporters.The Journal of general physiology · 2011Review
- Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.Annual review of biochemistry · 2011Review
- Molecular simulations of ion channels: a quantum chemist's perspective.The Journal of general physiology · 2010Article
- Computational analysis of membrane proteins: the largest class of drug targets.Drug discovery today · 2009Review
- Proton inhibition of unitary currents of vanilloid receptors.The Journal of general physiology · 2009Article
- Biomolecular simulation and modelling: status, progress and prospects.Journal of the Royal Society, Interface · 2008Review
- Conformational changes in the selectivity filter of the open-state KcsA channel: an energy minimization study.Biophysical journal · 2008Article
- Conformational dynamics of the KcsA potassium channel governs gating properties.Nature structural & molecular biology · 2007Article
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Authors and funding
3 authors.
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Abstract
Although a few x-ray structures of the KcsA K(+) channel have been crystallized several issues concerning the mechanisms of the ionic permeation and the protonation state of the selectivity filter ionizable side chains are still open. Using a first-principles quantum mechanical/molecular mechanical simulation approach, we have investigated the protonation state of Glu-71 and Asp-80, two important residues located in the vicinity of the selectivity filter. Results from the dynamics show that a proton is shared between the two residues, with a slight preference for Glu-71. The proton is found to exchange on the picosecond timescale, an interesting phenomenon that cannot be observed in classical molecular dynamics. Simulations of different ionic loading states of the filter show that the probability for the proton transfer is correlated with the filter occupancy. In addition, the Glu-71/Asp-80 pair is able to modulate the potential energy profile experienced by a K(+) ion as it translates along the pore axis. These theoretical predictions, along with recent experimental results, suggest that changes of the filter structure could be associated with a shift in the Glu-Asp protonation state, which in turn would influence the ion translocation.
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