Science. 1997 Dec 12;278(5345):1907-16.

Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS.

Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR.

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Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235-9050, USA.

Abstract

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.

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Pieces of the true grail: a G protein finds its target. [Science. 1997]
Pieces of the true grail: a G protein finds its target.Bourne HR. Science. 1997 Dec 12; 278(5345):1898-9.

PMID:: 9417641; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Complex Of Gs-Alpha With The Catalytic Domains Of Mammalian Adenylyl Cyclase

PDB: 1AZS

Source: Canis lupus familiaris, Rattus norvegicus, Bos taurus

Method: X-Ray Diffraction

Resolution: 2.3 Å

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