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 journalArticlepeer-review


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)
Pages (from-to)A1294
JournalFASEB Journal
Issue number9
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics


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