Braun Andrew P, Schriemer David C
Department of Physiology and Pharmacology, Faculty of Medicine, University of Calgary, 3330 Hospital Drive NW, Calgary, AB T2N 4N1, Canada.
Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Calgary, 3330 Hospital Drive NW, Calgary, AB T2N 4N1, Canada.
Structure. 2014 Apr 8;22(4):512-4. doi: 10.1016/j.str.2014.03.005.
The allosterically-induced outcome of nitric oxide (NO) binding to soluble guanylate cyclase (sGC) is well known but poorly understood. As described in this issue of Structure, Underbakke and coworkers apply a powerful hydrogen/deuterium exchange method to follow the key structural elements of the pathway between NO binding and sGC catalytic site activation.