Inhibition mechanisms of staurosporine and H7 to cAMP-dependent protein kinase through docking study

Chem Pharm Bull (Tokyo). 1996 Mar;44(3):618-20. doi: 10.1248/cpb.44.618.

Abstract

Inhibition mechanisms of staurosporine and H7 to cAMP-dependent protein kinase have been investigated through docking studies. For each molecule, the energetically most stable docking model was searched by using the conformationally flexible automatic docking program ADAM without any presumptions. The results explain well the observation that staurosporine does not bind to the enzyme competitively with H7, even though the two compounds competitively inhibit ATP binding.

MeSH terms

  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine / pharmacology*
  • Crystallization
  • Cyclic AMP-Dependent Protein Kinases / antagonists & inhibitors*
  • Cyclic AMP-Dependent Protein Kinases / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Protein Conformation
  • Staurosporine / pharmacology*

Substances

  • Enzyme Inhibitors
  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
  • Cyclic AMP-Dependent Protein Kinases
  • Staurosporine