Tracking allosteric propagation with HX-MS.
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.
Department of Physiology and Pharmacology, Faculty of Medicine, University of Calgary, 3330 Hospital Drive NW, Calgary, AB T2N 4N1, Canada.
Andrew P
AP
Braun
Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Calgary, 3330 Hospital Drive NW, Calgary, AB T2N 4N1, Canada. Electronic address: dschriem@ucalgary.ca.
David C
DC
Schriemer
D006152:Cyclic GMP / Q000737:chemistry*; D006162:Guanylate Cyclase / Q000737:chemistry*; D006801:Humans; D009569:Nitric Oxide / Q000737:chemistry*; D021122:Protein Subunits / Q000737:chemistry*; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry*; D000071756:Soluble Guanylyl Cyclase
D021122:Protein Subunits; D018160:Receptors, Cytoplasmic and Nuclear; D009569:Nitric Oxide; D006162:Guanylate Cyclase; D000071756:Soluble Guanylyl Cyclase; D006152:Cyclic GMP