ArticleThe Journal of biological chemistry2015
Pore hydration states of KcsA potassium channels in membranes.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Harnessing Membrane-Active Peptides for Selective Cancer Targeting: Phosphatidylserine Recognition by Tilapia Piscidin 4.JACS Au · 2026Article
- Water inside the Selectivity Filter of a KJournal of the American Chemical Society · 2024Article
- A governance of ion selectivity based on the occupancy of the "beacon" in one- and four-domain calcium and sodium channels.Channels (Austin, Tex.) · 2023Article
- Special issue for Klaus Gawrisch.Biophysical journal · 2023Article
- High-Resolution Structures of KHandbook of experimental pharmacology · 2021Article
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- The host-defense peptide piscidin P1 reorganizes lipid domains in membranes and decreases activation energies in mechanosensitive ion channels.The Journal of biological chemistry · 2019Article
- Why Nature Chose Potassium.Journal of molecular evolution · 2019Review
- Unambiguous observation of blocked states reveals altered, blocker-induced, cardiac ryanodine receptor gating.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
5 authors at 5 institutions in 1 country.
Funding
Abstract
Water-filled hydrophobic cavities in channel proteins serve as gateways for transfer of ions across membranes, but their properties are largely unknown. We determined water distributions along the conduction pores in two tetrameric channels embedded in lipid bilayers using neutron diffraction: potassium channel KcsA and the transmembrane domain of M2 protein of influenza A virus. For the KcsA channel in the closed state, the distribution of water is peaked in the middle of the membrane, showing water in the central cavity adjacent to the selectivity filter. This water is displaced by the channel blocker tetrabutyl-ammonium. The amount of water associated with the channel was quantified, using neutron diffraction and solid state NMR. In contrast, the M2 proton channel shows a V-shaped water profile across the membrane, with a narrow constriction at the center, like the hourglass shape of its internal surface. These two types of water distribution are therefore very different in their connectivity to the bulk water. The water and protein profiles determined here provide important evidence concerning conformation and hydration of channels in membranes and the potential role of pore hydration in channel gating.
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Registered trials
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