Research Article

Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in a Complex with G·GTPγS

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Science  12 Dec 1997:
Vol. 278, Issue 5345, pp. 1907-1916
DOI: 10.1126/science.278.5345.1907

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Abstract

The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein α subunit (Gs α) 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 Gs α.

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