Phe(475) and Glu(446) but not Ser(445) participate in ATP-binding to the alpha-subunit of Na(+)/K(+)-ATPase
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12220524
DOI
10.1016/s0006-291x(02)02089-2
PII: S0006291X02020892
Knihovny.cz E-zdroje
- MeSH
- adenosintrifosfát analogy a deriváty metabolismus MeSH
- fenylalanin metabolismus MeSH
- fluorescenční barviva metabolismus MeSH
- konformace proteinů MeSH
- kyselina glutamová metabolismus MeSH
- molekulární modely MeSH
- myši MeSH
- podjednotky proteinů MeSH
- rekombinantní fúzní proteiny metabolismus MeSH
- serin metabolismus MeSH
- sodíko-draslíková ATPasa metabolismus MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 2',3'-O-(2,4,6-trinitro-cyclohexadienylidine)adenosine 5'-triphosphate MeSH Prohlížeč
- adenosintrifosfát MeSH
- fenylalanin MeSH
- fluorescenční barviva MeSH
- kyselina glutamová MeSH
- podjednotky proteinů MeSH
- rekombinantní fúzní proteiny MeSH
- serin MeSH
- sodíko-draslíková ATPasa MeSH
The ATP-binding site of Na(+)/K(+)-ATPase is localized on the large cytoplasmic loop of the alpha-subunit between transmembrane helices H(4) and H(5). Site-directed mutagenesis was performed to identify residues involved in ATP binding. On the basis of our recently developed model of this loop, Ser(445), Glu(446), and Phe(475) were proposed to be close to the binding pocket. Replacement of Phe(475) with Trp and Glu(446) with Gln profoundly reduced the binding of ATP, whereas the substitution of Ser(445) with Ala did not affect ATP binding. Fluorescence measurements of the fluorescent analog TNP-ATP, however, indicated that Ser(445) is close to the binding site, although it does not participate in binding.
Citace poskytuje Crossref.org
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