Ion Pathways in the Na+/K+-ATPase

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F16%3A33160983" target="_blank" >RIV/61989592:15310/16:33160983 - isvavai.cz</a>
Result on the web
<a href="http://pubs.acs.org/doi/full/10.1021/acs.jcim.6b00353" target="_blank" >http://pubs.acs.org/doi/full/10.1021/acs.jcim.6b00353</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jcim.6b00353" target="_blank" >10.1021/acs.jcim.6b00353</a>

Result language
angličtina
Original language name
Ion Pathways in the Na+/K+-ATPase
Original language description
We report molecular dynamic simulations of the human Na+ /K+ -ATPase α1β1 isoform embedded into DOPC bilayer. We have analyzed the Na+ /K+ -ATPase conformational changes in the presence of Na+- or K+-cations in the cation binding site, for various combinations of the cytoplasmic ligands, and the two major enzyme conformations. We identified two novel cytoplasmic pathways along the pairs of transmembrane helices TM3/TM7 or TM6/TM9 that allow hydration of the cation binding site or transport of cations from/to the bulk. These findings can provide a structural explanation for previous mutagenesis studies, where mutation of residues that are distal from the cation binding site resulted in the alteration of the enzyme affinity to the transported cations or change in the enzyme activity.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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