RH421 binds into the ATP-binding site on the Na+/K+-ATPase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F17%3A00485540" target="_blank" >RIV/68081707:_____/17:00485540 - isvavai.cz</a>
Alternative codes found
RIV/00159816:_____/17:00068489 RIV/61989592:15310/17:73582666
Result on the web
<a href="http://dx.doi.org/10.1016/j.bbamem.2017.07.016" target="_blank" >http://dx.doi.org/10.1016/j.bbamem.2017.07.016</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bbamem.2017.07.016" target="_blank" >10.1016/j.bbamem.2017.07.016</a>
Alternative languages
Result language
angličtina
Original language name
RH421 binds into the ATP-binding site on the Na+/K+-ATPase
Original language description
The Na+/K+-ATPase plays a key role in ion transport across the plasma membrane of all animal cells. The voltage-sensitive styrylpyrimidium dye RH421 has been used in several laboratories for monitoring of Na+/K+-ATPase kinetics. It is known, that RH421 can interact with the enzyme and it can influence its activity at micromolar concentrations, but structural details of this interaction are only poorly understood. Experiments with isolated large cytoplasmic loop (C45) of Na+/K+-ATPase revealed that RH421 can interact with this part of the protein with dissociation constant 1 mu M. The Trp-to-RH421 FRET performed on six single-tryptophan mutants revealed that RH421 binds directly into the ATP-binding site. This conclusion was further supported by results from molecular docking, site-directed mutagenesis and by competitive experiments using ATP. Experiments with C45/DPPC mixture revealed that RH421 can bind to both C45 and lipids, but only the former interaction was influenced by the presence of ATP.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochimica Et Biophysica Acta-Biomembranes
ISSN
0005-2736
e-ISSN
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Volume of the periodical
1859
Issue of the periodical within the volume
10
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
10
Pages from-to
2113-2122
UT code for WoS article
000411419000036
EID of the result in the Scopus database
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