NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region
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The structure of a synthetic peptide corresponding to the fifth membrane-spanning segment (M5) in Na(+),K(+)-ATPase in sodium dodecyl sulfate (SDS) micelles was determined using liquid-state nuclear magnetic resonance (NMR) spectroscopy. The spectra reveal that this peptide is substantially less alpha-helical than the corresponding M5 peptide of Ca(2+)-ATPase. A well-defined alpha-helix is shown in the C-terminal half of the peptide. Apart from a short helical stretch at the N-terminus, the N-terminal half contains a non-helical region with two proline residues and sequence similarity to a non-structured transmembrane element of the Ca(2+)-ATPase. Furthermore, this region spans the residues implicated in Na(+) and K(+) transport, where they are likely to offer the flexibility needed to coordinate Na(+) as well as K(+) during active transport.
Original language | English |
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Journal | FEBS Letters |
Volume | 580 |
Issue number | 20 |
Pages (from-to) | 4777-83 |
Number of pages | 7 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 4 Sep 2006 |
- Amino Acid Sequence, Humans, Ions, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptides, Potassium, Protein Structure, Secondary, Protein Structure, Tertiary, Sodium, Sodium-Potassium-Exchanging ATPase
Research areas
ID: 112952519