Camp-dependent protein kinase: Structural basis for activation and subcellular localization

S. S. Tavlor, N. Naravana, J. Lew, X. Cheng, W. Wen, R. Aimes, R. M. Gibson, L. J. Huang

Research output: Contribution to journalArticle

Abstract

cAMP-dependent protein kinase (cAPK) is one of the simplest members of the protein kinase family and has served in many ways as a prototype for all eukaryotic protein kinases. The structure of the catalytic (C) subunit coupled with a detailed dissecting of the kinetics of the phosphoryl transfer reaction has defined a dynamic set of steps that correlate opening and closing of the active site cleft with phosphoryl transfer and product release. The structure and mutational analysis of the inhibitors of the C-subunit, both the regulatory subunits and the heat stable protein kinase inhibitors, have revealed diversity in how the C-subunit uses different surfaces to achieve high affinity binding of its different classes of inhibitors. The modular and multifunctional nature of these inhibitors are defining a broad scope for the role that they play in the trafficking and subcellular localization of cAPK.

Original languageEnglish (US)
JournalFASEB Journal
Volume11
Issue number9
StatePublished - 1997

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ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Tavlor, S. S., Naravana, N., Lew, J., Cheng, X., Wen, W., Aimes, R., Gibson, R. M., & Huang, L. J. (1997). Camp-dependent protein kinase: Structural basis for activation and subcellular localization. FASEB Journal, 11(9).