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Crystallographic Studies of the Catalytic Subunit of cAMP- Dependent Protein Kinase

  • Daniel R. Knighton
  • Jianhua Zheng
  • Victor A. Ashford
  • Susan S. Taylor
  • Nguyen-huu Xuong
  • Janusz M. Sowadski
Conference paper
Part of the NATO ASI Series book series (volume 56)

Abstract

The cAMP-dependent protein kinase (reviewed in Beebe and Corbin, 1986) is a tetrameric enzyme, probably ubiquitous in eukaryotic cells, composed of two regulatory and two catalytic (C) subunits. Upon binding cAMP the regulatory dimer releases two monomeric C-subunits, which then use MgATP to phosphorylate serine or threonine residues found typically in the sequence Arg-Arg-X-Ser/Thr in target proteins. Protein phosphorylation is a well-known mechanism for regulating protein function (reviewed in Krebs, 1985), and a large number of proteins have been found whose activity the C-subunit regulates this way, including many from the glycolytic and gluconeogenetic pathways (Krebs, 1985).

Keywords

Catalytic Subunit Nucleotide Binding Site Dependent Protein Kinase Porcine Heart Hexagonal Form 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Daniel R. Knighton
    • 1
  • Jianhua Zheng
    • 1
  • Victor A. Ashford
    • 2
  • Susan S. Taylor
    • 1
  • Nguyen-huu Xuong
    • 1
    • 2
    • 3
  • Janusz M. Sowadski
    • 4
  1. 1.Department of ChemistryUniversity of California, San DiegoLa JollaUSA
  2. 2.Department of BiologyUniversity of California, San DiegoLa JollaUSA
  3. 3.Department of PhysicsUniversity of California, San Diego9500 Gilman DriveLa JollaUSA
  4. 4.Department of MedicineUniversity of California, San DiegoLa JollaUSA

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