Eight amino acids form the ATP recognition site of Na(+)/K(+)-ATPase
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12767226
DOI
10.1021/bi034162u
Knihovny.cz E-resources
- MeSH
- Adenosine Triphosphate metabolism MeSH
- Amino Acids chemistry MeSH
- Point Mutation MeSH
- Cysteine chemistry MeSH
- Phenylalanine chemistry MeSH
- Genetic Vectors MeSH
- Glutamine chemistry MeSH
- Glutamic Acid chemistry MeSH
- Models, Molecular MeSH
- Brain enzymology MeSH
- Mutagenesis, Site-Directed MeSH
- Mice MeSH
- Recombinant Fusion Proteins chemistry metabolism MeSH
- Recombinant Proteins chemistry MeSH
- Protein Structure, Secondary MeSH
- Sodium-Potassium-Exchanging ATPase chemistry MeSH
- Spectrophotometry, Infrared MeSH
- Spectroscopy, Fourier Transform Infrared MeSH
- Genetic Complementation Test MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Hydrogen Bonding MeSH
- Dose-Response Relationship, Drug 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
- Adenosine Triphosphate MeSH
- Amino Acids MeSH
- Cysteine MeSH
- Phenylalanine MeSH
- Glutamine MeSH
- Glutamic Acid MeSH
- Recombinant Fusion Proteins MeSH
- Recombinant Proteins MeSH
- Sodium-Potassium-Exchanging ATPase MeSH
Point mutations of a part of the H(4)-H(5) loop (Leu(354)-Ile(604)) of Na(+)/K(+)-ATPase have been used to study the ATP and TNP-ATP binding affinities. Besides the previously reported amino acid residues Lys(480), Lys(501), Gly(502), and Cys(549), we have found four more amino acid residues, viz., Glu(446), Phe(475), Gln(482), and Phe(548), completing the ATP-binding pocket of Na(+)/K(+)-ATPase. Moreover, mutation of Arg(423) has also resulted in a large decrease in the extent of ATP binding. This residue, localized outside the binding pocket, seems to play a key role in supporting the proper structure and shape of the binding site, probably due to formation of a hydrogen bond with Glu(472). On the other hand, only some minor effects were caused by mutations of Ile(417), Asn(422), Ser(445), and Glu(505).
References provided by Crossref.org
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