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Crystal structure of the sodium–potassium pump at 2.4 Å resolution

Takehiro Shinoda, Haruo Ogawa, Flemming Cornelius and Chikashi Toyoshima ()
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Takehiro Shinoda: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan
Haruo Ogawa: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan
Flemming Cornelius: University of Aarhus
Chikashi Toyoshima: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan

Nature, 2009, vol. 459, issue 7245, 446-450

Abstract: Na+, K+-ATPase structure The sodium-potassium ATPase is an ATP-powered ion pump that creates concentration gradients for sodium and potassium ions across the plasma membrane of animal cells. Sodium ions are exported from the cell while potassium ions are imported producing gradients that are used for many essential processes, such as the action potentials of nerve cells. The crystal structure of this protein from shark rectal gland — highly homologous to the human version — has now been determined at 2.4 Å resolution. The structure helps elucidate many details of the protein's mechanism of action and will contribute, among other things, to the understanding and treatment of heart disease, since cardiac glycosides are inhibitors of the sodium-potassium pump.

Date: 2009
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DOI: 10.1038/nature07939

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