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- Title
NMR studies of the fifth transmembrane segment of Na<sup>+</sup>,K<sup>+</sup>-ATPase reveals a non-helical ion-binding region
- Authors
Underhaug, Jarl; Jakobsen, Louise Odgaard; Esmann, Mikael; Malmendal, Anders; Nielsen, Niels Chr.
- Abstract
Abstract: 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 α-helical than the corresponding M5 peptide of Ca2+-ATPase. A well-defined α-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 Ca2+-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.
- Subjects
ADENOSINE triphosphatase; MAGNETIC fields; MEMBRANE proteins; MAGNETIC resonance
- Publication
FEBS Letters, 2006, Vol 580, Issue 20, p4777
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2006.07.063