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Differential ion dehydration energetics explains selectivity in the non-canonical lysosomal K <sup>+</sup> channel TMEM175

2021-11-06

Abstract excerpt

Structures of the human lysosomal K + channel TMEM175 in open and closed states revealed a novel architecture lacking the canonical K + selectivity filter motif present in previously known K + channel structures. A hydrophobic constriction composed of four isoleucine residues was resolved in the pore and proposed to serve as the gate in the closed state, and to confer ion selectivity in the open state. Here, we...

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Literature Corpus work
de8a2551-fd00-5231-87ab-95be7316db3d
DOI
10.1101/2021.11.05.467414
Open publication

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Differential ion dehydration energetics explains selectivity in the non-canonical lysosomal K <sup>+</sup> channel TMEM175DOI 10.1101/2021.11.05.467414
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