Na+/H+ antiporters finely tune intracellular concentrations of salt and pH by rapidly exchanging sodium ions with protons across the cell membrane. In humans these integral membrane proteins play an important role in physiology and their dysfunction is associated with a number of different diseases, eg, postischemic myocardial arrhythmias, cancer, heart disease and hypertension, the latter a major disorder affecting 1 in 4 adults in the United States. Here, I will discuss new structural insights into the mechanics of Na+/H+ antiport that has enabled us to have a better understanding of how they function at the atomic level.
37th Congress of IUPS (Birmingham, UK) (2013) Proc 37th IUPS, SA364
Research Symposium: The mechanics of Na+/H+ antiport
D. Drew1,2, C. Lee1, H. Kang1, C. von Ballmoos2, S. Newstead1,4, P. Uzdavinys2, S. Iwata3,4, O. Beckstein5, A. Cameron3,4
1. Molecular Biosciences, Imperial College London, London, United Kingdom. 2. Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. 3. Membrane Protein Laboratory, Diamond Light Source, Harwell, United Kingdom. 4. Research Complex at Harwell Rutherford, Appleton Laboratory, Harwell, United Kingdom. 5. Department of Physics, Arizona State University, Tempe, Arizona, United States.
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