Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in a Complex with G sα ·GTPγS-Reference-Cited by-同舟云学术

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

Published:1997-12-12 Issue:5345 Volume:278 Page:1907-1916
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Tesmer John J. G.¹,Sunahara Roger K.¹,Gilman Alfred G.¹,Sprang Stephen R.¹

Affiliation:

1. J. J. G. Tesmer and S. R. Sprang are at the Howard Hughes Medical Institute and the Department of Biochemistry, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235–9050, USA. R. K. Sunahara and A. G. Gilman are in the Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235–9041, USA.

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 s 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 G s α .

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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