Tesmer J J, Sunahara R K, Gilman A G, Sprang S R
Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235-9050, USA.
Science. 1997 Dec 12;278(5345):1907-16. doi: 10.1126/science.278.5345.1907.
The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein alpha subunit (Gsalpha) and forskolin was determined to a resolution of 2.3 angstroms. When P-site inhibitors were soaked into native crystals of the complex, the active site of adenylyl cyclase was located and structural elements important for substrate recognition and catalysis were identified. On the basis of these and other structures, a molecular mechanism is proposed for the activation of adenylyl cyclase by Gsalpha.
测定了一种可溶性、具有催化活性的腺苷酸环化酶与其刺激性异源三聚体G蛋白α亚基（Gsα）和福斯可林形成复合物的晶体结构，分辨率为2.3埃。当将P位点抑制剂浸泡到该复合物的天然晶体中时，确定了腺苷酸环化酶的活性位点，并鉴定了对底物识别和催化重要的结构元件。基于这些及其他结构，提出了一种Gsα激活腺苷酸环化酶的分子机制。
