Interactions of LY333531 and other bisindolyl maleimide inhibitors with PDK1

Structure. 2004 Feb;12(2):215-26. doi: 10.1016/j.str.2004.01.005.

Abstract

LY333531, BIM-1, BIM-2, BIM-3, and BIM-8 are bisindolyl maleimide-based, nanomolar protein kinase C inhibitors. LY333531, a PKCbeta-specific inhibitor, is in clinical trials against diabetes and cardiac ventricular hypertrophy complications. Specificity analysis with a panel of 29 protein kinases reveals that these bisindolyl maleimide inhibitors also inhibit PDK1, a key kinase from the insulin signaling pathway, albeit in the lower microM range. To understand the molecular basis of inhibition, the PDK1 kinase domain was cocrystallized with these bisindolyl maleimide inhibitors. The inhibitor complexes represent the first structural description of this class of compounds, revealing their unusual nonplanar conformation within the ATP binding site and also explaining the higher inhibitory potential of LY33331 compared to the BIM compounds toward PDK1. A combination of site-directed mutagenesis and essential dynamics analysis gives further insight into PDK1 and also PKC inhibition by these compounds, and may aid inhibitor design.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Phosphoinositide-Dependent Protein Kinases
  • Binding Sites
  • Crystallography, X-Ray
  • Enzyme Inhibitors / pharmacology
  • Indoles / pharmacology*
  • Maleimides / pharmacology*
  • Models, Molecular*
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism
  • Protein Serine-Threonine Kinases / antagonists & inhibitors
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Structure, Tertiary
  • Signal Transduction

Substances

  • Enzyme Inhibitors
  • Indoles
  • Maleimides
  • 3-Phosphoinositide-Dependent Protein Kinases
  • Protein Serine-Threonine Kinases
  • Protein Kinase C
  • bisindolylmaleimide

Associated data

  • PDB/1UU3
  • PDB/1UU7
  • PDB/1UU8
  • PDB/1UU9
  • PDB/1UVR