Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F02%3A00007337" target="_blank" >RIV/00216208:11310/02:00007337 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase
Original language description
The ATP-binding site of Na+/K+-ATPase is localized on the large cytoplasmic loop of the small alpha, Greek-subunit between transmembrane helices H4 and H5. Site-directed mutagenesis was performed to identify residues involved in ATP binding. On the basisof our recently developed model of this loop, Ser445, Glu446, and Phe475 were proposed to be close to the binding pocket. Replacement of Phe475 with Trp and Glu446 with Gln profoundly reduced the binding of ATP, whereas the substitution of Ser445 with Ala did not affect ATP binding. Fluorescence measurements of the fluorescent analog TNP-ATP, however, indicated that Ser445 is close to the binding site, although it does not participate in binding
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
CE - Biochemistry
OECD FORD branch
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Project
<a href="/en/project/LN00A026" target="_blank" >LN00A026: Center of molecular and cellular immunology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2002
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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