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.

I: FEBS Letters, Bind 580, Nr. 20, 04.09.2006, s. 4777-83.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Underhaug, J, Jakobsen, LO, Esmann, M, Malmendal, A & Nielsen, NC 2006, 'NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region', FEBS Letters, bind 580, nr. 20, s. 4777-83. https://doi.org/10.1016/j.febslet.2006.07.063

APA

Underhaug, J., Jakobsen, L. O., Esmann, M., Malmendal, A., & Nielsen, N. C. (2006). NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region. FEBS Letters, 580(20), 4777-83. https://doi.org/10.1016/j.febslet.2006.07.063

Vancouver

Underhaug J, Jakobsen LO, Esmann M, Malmendal A, Nielsen NC. NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region. FEBS Letters. 2006 sep. 4;580(20):4777-83. https://doi.org/10.1016/j.febslet.2006.07.063

Author

Underhaug, Jarl ; Jakobsen, Louise Odgaard ; Esmann, Mikael ; Malmendal, Anders ; Nielsen, Niels Chr. / NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region. I: FEBS Letters. 2006 ; Bind 580, Nr. 20. s. 4777-83.

Bibtex

@article{e06bd3509b97413c8dbea396bfb58539,
title = "NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region",
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 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.",
keywords = "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",
author = "Jarl Underhaug and Jakobsen, {Louise Odgaard} and Mikael Esmann and Anders Malmendal and Nielsen, {Niels Chr}",
year = "2006",
month = sep,
day = "4",
doi = "10.1016/j.febslet.2006.07.063",
language = "English",
volume = "580",
pages = "4777--83",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "20",

}

RIS

TY - JOUR

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