Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding-Reference-Cited by-同舟云学术

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Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding

Published:2014-06-04 Issue:1 Volume:4 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Petrushanko Irina Yu.,Mitkevich Vladimir A.,Anashkina Anastasia A.,Klimanova Elizaveta A.,Dergousova Elena A.,Lopina Olga D.,Makarov Alexander A.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep05165.pdf

Reference34 articles.

1. Schainer-Bobis, G. The sodium pump. Its molecular properties and mechanics of ion transport. Eur. J. Biochem. 269, 2424–2433 (2002).

2. Apell, H. J. & Karlish, S. J. Functional properties of Na,K-ATPase and their structural implications, as detected with biophysical techniques. J. Membr. Biol. 180, 1–9 (2001).

3. Geering, K. The functional role of beta subunits in oligomeric P-type ATPases. J. Bioenerg. Biomembr. 33, 425–438 (2001).

4. Nyblom, M. et al. Crystal structure of Na+, K(+)-ATPase in the Na(+)-bound state. Science 342, 123–127 (2013).

5. Kanai, R., Ogawa, H., Vilsen, B., Cornelius, F. & Toyoshima, C. Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state. Nature 502, 201–206 (2013).

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