Fluorone dyes have binding sites on both cytoplasmic and extracellular domains of Na,K-ATPase

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33145503" target="_blank" >RIV/61989592:15310/13:33145503 - isvavai.cz</a>
Result on the web
<a href="http://www.sciencedirect.com/science/article/pii/S0005273612003781" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0005273612003781</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bbamem.2012.10.029" target="_blank" >10.1016/j.bbamem.2012.10.029</a>

Result language
angličtina
Original language name
Fluorone dyes have binding sites on both cytoplasmic and extracellular domains of Na,K-ATPase
Original language description
Combination of fluorescence techniques and molecular docking was used to monitor interaction of Na,K-ATPase and its large cytoplasmic loop connecting fourth and fifth transmembrane helices (C45) with fluorone dyes (i.e. eosin Y, 5(6)-carboxyeosin, rose bengal, fluorescein, and erythrosine B). Our data suggested that there are at least two binding sites for all used fluorone dyes, except of 5(6)-carboxyeosin. The first binding site is located on C45 loop, and it is sensitive to the presence of nucleotide. The other site is located on the extracellular part of the enzyme, and it is sensitive to the presence of Na + or K+ ions.
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
BO - Biophysics
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)

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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