Na+/K+-ATPase (NKA) is a membrane protein that transports Na+ ions out of the cell and brings K+ ions into the cell against their concentration gradient. To function, NKA harnesses the chemical energy stored in an ATP molecule to cycle between two major conformational states during active pumping: a high affinity state for Na+, and a high affinity state for K+. The recent availability of the crystal structures  for these states, now makes it possible to computationally determine the factors that control selectivity for Na+ versus K+ ions. High selectivity of NKA for Na+ or K+ may be a result of thermodynamic (different affinities for binding sites) as well as kinetic (barriers along binding pathways) factors.
- Journal article: Molecular simulations and free-energy calculations suggest conformation-dependent anion binding to a cytoplasmic site as a mechanism for Na+/K+-ATPase ion selectivity, Asghar M Razavi, Lucie Delemotte, Joshua R Berlin, Vincenzo Carnevale, and Vincent A Voelz, Journal of Biological Chemistry 292: 12412-12423, 2017 [PDF]
- Conference talk: Razavi, A. M., Carnevale, V., Delemotte, L., & Voelz, V.A. (2015, February 9). Understanding selectivity of the Na+/K+ -ATPase using a computational approach. Platform presentation conducted at the meeting of the Biophysical Society, Baltimore, MD. http://cld.bz/kbr001i#68/z
- Poster: Razavi, A. M., Delemotte, L., Carnevale, V., & Voelz, V.A. (2015, June). Understanding selectivity of Na+/K+-ATPase by computational approach. Poster presented at the Gordon Research Conference, Lewiston, ME. [PDF]
- Poster: Razavi, A. M., Delemotte, L., Carnevale, V., & Voelz, V.A. (2015, May). Understanding selectivity of Na+/K+ -ATPase by computational approach. Poster presented at the Protein Folding Consortium Workshop, Berkeley, CA. [PDF]