Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G(sα)·GTPγΣ

Authors

John J.G. Tesmer, Howard Hughes Medical Institute
Roger K. Sunahara, University of Texas Southwestern Medical Center
Alfred G. Gilman, University of Texas Southwestern Medical Center
Stephen R. Sprang, University of Montana

Document Type

Article

Publication Title

Science

Publication Date

12-12-1997

Volume

278

Issue

5345

Disciplines

Biology | Life Sciences

Abstract

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

DOI

https://doi.org/10.1126/science.278.5345.1907

Recommended Citation

Tesmer, John J.G.; Sunahara, Roger K.; Gilman, Alfred G.; and Sprang, Stephen R., "Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G(sα)·GTPγΣ" (1997). Biological Sciences Faculty Publications. 537.
https://scholarworks.umt.edu/biosci_pubs/537