کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2052473 1074231 2006 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 20, 4 September 2006, Pages 4777–4783
نویسندگان
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