Phe(475) and Glu(446) but not Ser(445) participate in ATP-binding to the alpha-subunit of Na(+)/K(+)-ATPase
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12220524
DOI
10.1016/s0006-291x(02)02089-2
PII: S0006291X02020892
Knihovny.cz E-resources
- MeSH
- Adenosine Triphosphate analogs & derivatives metabolism MeSH
- Phenylalanine metabolism MeSH
- Fluorescent Dyes metabolism MeSH
- Protein Conformation MeSH
- Glutamic Acid metabolism MeSH
- Models, Molecular MeSH
- Mice MeSH
- Protein Subunits MeSH
- Recombinant Fusion Proteins metabolism MeSH
- Serine metabolism MeSH
- Sodium-Potassium-Exchanging ATPase metabolism MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 2',3'-O-(2,4,6-trinitro-cyclohexadienylidine)adenosine 5'-triphosphate MeSH Browser
- Adenosine Triphosphate MeSH
- Phenylalanine MeSH
- Fluorescent Dyes MeSH
- Glutamic Acid MeSH
- Protein Subunits MeSH
- Recombinant Fusion Proteins MeSH
- Serine MeSH
- Sodium-Potassium-Exchanging ATPase 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.
References provided by Crossref.org
Identification of cisplatin-binding sites on the large cytoplasmic loop of the Na+/K+-ATPase
