Structure prediction and validation of the ERK8 kinase domain

PLoS One. 2013;8(1):e52011. doi: 10.1371/journal.pone.0052011. Epub 2013 Jan 11.

Abstract

Extracellular signal-regulated kinase 8 (ERK8) has been already implicated in cell transformation and in the protection of genomic integrity and, therefore, proposed as a novel potential therapeutic target for cancer. In the absence of a crystal structure, we developed a three-dimensional model for its kinase domain. To validate our model we applied a structure-based virtual screening protocol consisting of pharmacophore screening and molecular docking. Experimental characterization of the hit compounds confirmed that a high percentage of the identified scaffolds was able to inhibit ERK8. We also confirmed an ATP competitive mechanism of action for the two best-performing molecules. Ultimately, we identified an ERK8 drug-resistant "gatekeeper" mutant that corroborated the predicted molecular binding mode, confirming the reliability of the generated structure. We expect that our model will be a valuable tool for the development of specific ERK8 kinase inhibitors.

Publication types

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

MeSH terms

  • Adenosine Diphosphate / chemistry
  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Binding Sites / genetics
  • Biocatalysis / drug effects
  • Blotting, Western
  • Extracellular Signal-Regulated MAP Kinases / chemistry*
  • Extracellular Signal-Regulated MAP Kinases / genetics
  • Extracellular Signal-Regulated MAP Kinases / metabolism*
  • Humans
  • Models, Molecular*
  • Molecular Dynamics Simulation
  • Molecular Sequence Data
  • Molecular Structure
  • Mutation
  • Protein Binding
  • Protein Kinase Inhibitors / chemistry
  • Protein Kinase Inhibitors / metabolism
  • Protein Kinase Inhibitors / pharmacology
  • Protein Structure, Tertiary*
  • Sequence Homology, Amino Acid

Substances

  • Protein Kinase Inhibitors
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Extracellular Signal-Regulated MAP Kinases
  • MAPK15 protein, human

Grants and funding

This work was supported by a Start-up grant from Regione Toscana and by a grant to Regione Toscana from Ministero della Salute, in the context of the “Programma per la Ricerca Sanitaria 2008: Bando Cellule Staminali”. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.