A template for the protein kinase family

Trends Biochem Sci. 1993 Mar;18(3):84-9. doi: 10.1016/0968-0004(93)80001-r.


The crystal structure of the catalytic subunit of cAMP-dependent protein kinase, complexed with ATP and a 20-residue inhibitor peptide, is reviewed and correlated with chemical and genetic data. The striking convergence of the structure with the biochemistry and genetics provides for the first time a molecular basis for understanding how this enzyme functions, as well as an explanation for the highly conserved residues that are scattered throughout the molecule. Because these residues probably serve a common role in all eukaryotic protein kinases, this first protein kinase structure serves as a general template for the entire family of enzymes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Molecular Sequence Data
  • Mutation
  • Protein Kinases / chemistry*
  • Protein Kinases / genetics
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Structure-Activity Relationship


  • Protein Kinases