Change search
ReferencesLink to record
Permanent link

Direct link
Crystal Structure of Na+, K+-ATPase in the Na+-Bound State
Show others and affiliations
2013 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 342, no 6154, 123-127 p.Article in journal (Refereed) Published
Abstract [en]

The Na+, K+-adenosine triphosphatase (ATPase) maintains the electrochemical gradients of Na+ and K+ across the plasma membrane-a prerequisite for electrical excitability and secondary transport. Hitherto, structural information has been limited to K+-bound or ouabain-blocked forms. We present the crystal structure of a Na+-bound Na+, K+-ATPase as determined at 4.3 angstrom resolution. Compared with the K+-bound form, large conformational changes are observed in the a subunit whereas the beta and gamma subunit structures are maintained. The locations of the three Na+ sites are indicated with the unique site III at the recently suggested IIIb, as further supported by electrophysiological studies on leak currents. Extracellular release of the third Na+ from IIIb through IIIa, followed by exchange of Na+ for K+ at sites I and II, is suggested.

Place, publisher, year, edition, pages
2013. Vol. 342, no 6154, 123-127 p.
National Category
Biological Sciences
URN: urn:nbn:se:su:diva-95747DOI: 10.1126/science.1243352ISI: 000325126100060OAI: diva2:662282


Available from: 2013-11-06 Created: 2013-11-04 Last updated: 2013-11-06Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Lindahl, Erik
By organisation
Department of Biochemistry and BiophysicsScience for Life Laboratory (SciLifeLab)
In the same journal
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 24 hits
ReferencesLink to record
Permanent link

Direct link