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  Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling.

Kopec, W., Rothberg, B. S., & de Groot, B. L. (2019). Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling. Nature Communications, 10: 5366. doi:10.1038/s41467-019-13227-w.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-5393-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-5397-3
Genre: Journal Article

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Kopec, W.1, Author              
Rothberg, B. S., Author
de Groot, B. L.1, Author              
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1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              

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 Abstract: Potassium channels are presumed to have two allosterically coupled gates, the activation gate and the selectivity filter gate, that control channel opening, closing, and inactivation. However, the molecular mechanism of how these gates regulate K+ ion flow through the channel remains poorly understood. An activation process, occurring at the selectivity filter, has been recently proposed for several potassium channels. Here, we use X-ray crystallography and extensive molecular dynamics simulations, to study ion permeation through a potassium channel MthK, for various opening levels of both gates. We find that the channel conductance is controlled at the selectivity filter, whose conformation depends on the activation gate. The crosstalk between the gates is mediated through a collective motion of channel helices, involving hydrophobic contacts between an isoleucine and a conserved threonine in the selectivity filter. We propose a gating model of selectivity filter-activated potassium channels, including pharmacologically relevant two-pore domain (K2P) and big potassium (BK) channels.

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Language(s): eng - English
 Dates: 2019-11-26
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-019-13227-w
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Title: Nature Communications
Source Genre: Journal
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Pages: 15 Volume / Issue: 10 Sequence Number: 5366 Start / End Page: - Identifier: -