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

DOI Web Site 被引用文献14件
  • John J. G. Tesmer
    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.
  • Roger K. Sunahara
    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.
  • Alfred G. Gilman
    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.
  • Stephen R. Sprang
    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.

抄録

<jats:p> The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein α subunit (G <jats:sub>s</jats:sub> <jats:sub>α</jats:sub> ) 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 <jats:sub>s</jats:sub> <jats:sub>α</jats:sub> . </jats:p>

収録刊行物

  • Science

    Science 278 (5345), 1907-1916, 1997-12-12

    American Association for the Advancement of Science (AAAS)

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