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Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS.,Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR Science. 1997 Dec 12;278(5345):1907-16. PMID:9417641[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR. Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS. Science. 1997 Dec 12;278(5345):1907-16. PMID:9417641
