NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region
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NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region. / Underhaug, Jarl; Jakobsen, Louise Odgaard; Esmann, Mikael; Malmendal, Anders; Nielsen, Niels Chr.
In: FEBS Letters, Vol. 580, No. 20, 04.09.2006, p. 4777-83.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region
AU - Underhaug, Jarl
AU - Jakobsen, Louise Odgaard
AU - Esmann, Mikael
AU - Malmendal, Anders
AU - Nielsen, Niels Chr
PY - 2006/9/4
Y1 - 2006/9/4
N2 - 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.
AB - 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.
KW - Amino Acid Sequence
KW - Humans
KW - Ions
KW - Models, Molecular
KW - Molecular Sequence Data
KW - Nuclear Magnetic Resonance, Biomolecular
KW - Peptides
KW - Potassium
KW - Protein Structure, Secondary
KW - Protein Structure, Tertiary
KW - Sodium
KW - Sodium-Potassium-Exchanging ATPase
U2 - 10.1016/j.febslet.2006.07.063
DO - 10.1016/j.febslet.2006.07.063
M3 - Journal article
C2 - 16904671
VL - 580
SP - 4777
EP - 4783
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 20
ER -
ID: 112952519