Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2

Nat Struct Biol. 1997 Oct;4(10):796-801. doi: 10.1038/nsb1097-796.

Abstract

Staurosporine exhibits nanomolar IC50 values against a wide range of protein kinases. The structure of a CDK2 staurosporine complex explains the tight binding of this inhibitor, and suggests features to be exploited in the design of specific inhibitors of CDKs.

Publication types

  • Comparative Study
  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CDC2-CDC28 Kinases*
  • Crystallography, X-Ray
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases / antagonists & inhibitors*
  • Cyclin-Dependent Kinases / biosynthesis
  • Cyclin-Dependent Kinases / chemistry*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Models, Molecular
  • Molecular Conformation
  • Molecular Sequence Data
  • Protein Conformation*
  • Protein Kinases / chemistry*
  • Protein Serine-Threonine Kinases / antagonists & inhibitors*
  • Protein Serine-Threonine Kinases / biosynthesis
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Structure, Secondary
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Reproducibility of Results
  • Sequence Alignment
  • Spodoptera
  • Staurosporine / chemistry*
  • Staurosporine / pharmacology*
  • Transfection

Substances

  • Enzyme Inhibitors
  • Recombinant Proteins
  • Protein Kinases
  • Protein Serine-Threonine Kinases
  • CDC2-CDC28 Kinases
  • CDK2 protein, human
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases
  • Staurosporine