Structural insights into the mechanism of human soluble guanylate cyclase

• Published in: Nature (London) Vol. 574; no. 7777; pp. 206 - 210
• Main Authors: Kang, Yunlu, Liu, Rui, Wu, Jing-Xiang, Chen, Lei
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.10.2019; Nature Publishing Group
• Subjects: 101/28; 631/443/1338/1872; 631/45/607; 631/535/1258/1259; 631/80/86; 692/699/75; 82/16; 82/29; 82/80; 82/83; Angina pectoris; Animals; Binding; Catalysis; Cryoelectron Microscopy; Disease; Disulfides - chemistry; Disulfides - metabolism; Domains; Drosophila melanogaster; Electron microscopy; Enzymatic activity; Enzyme Activation; Guanylate cyclase; Health aspects; HEK293 Cells; Heme - metabolism; Humanities and Social Sciences; Humans; Hydrazines - pharmacology; Kinases; Mice; Microscopy; Models, Molecular; Modules; multidisciplinary; Nitric oxide; Nitric Oxide - metabolism; Nitric Oxide Donors - metabolism; Oxygen; Oxygen - metabolism; Physiological aspects; Physiology; Protein Domains; Protein Multimerization; Protein research; Proteins; Science; Science (multidisciplinary); Sensors; Soluble Guanylyl Cyclase - chemistry; Soluble Guanylyl Cyclase - genetics; Soluble Guanylyl Cyclase - metabolism; Soluble Guanylyl Cyclase - ultrastructure; Structure; China

Soluble guanylate cyclase (sGC) is the primary sensor of nitric oxide. It has a central role in nitric oxide signalling and has been implicated in many essential physiological processes and disease conditions. The binding of nitric oxide boosts the enzymatic activity of sGC. However, the mechanism b...