Theoretical analysis of the binding of potential inhibitors to protein kinases MK2 and MK3

Med Chem. 2015;11(6):573-9. doi: 10.2174/1573406411666150209114952.

Abstract

MK2 (or MAPKAPK2) was already known for its role in the inflammatory response, however recent studies indicate the involvement of this protein kinase in the DNA damage response mechanism. Within its kinase family the enzyme MK3 shows the highest identity with MK2. Here we report a theoretical study on the binding of two molecules, 05B and P4O, to the proteins MK2 and MK3. The data here obtained may shed light on the contribution of individual residues and binding site water molecules for the binding of potential inhibitors to these two kinases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Dose-Response Relationship, Drug
  • Humans
  • Intracellular Signaling Peptides and Proteins / antagonists & inhibitors*
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Models, Molecular
  • Molecular Structure
  • Protein Binding
  • Protein Kinase Inhibitors / chemical synthesis
  • Protein Kinase Inhibitors / chemistry
  • Protein Kinase Inhibitors / metabolism*
  • Protein Kinase Inhibitors / pharmacology*
  • Protein Serine-Threonine Kinases / antagonists & inhibitors*
  • Protein Serine-Threonine Kinases / metabolism*
  • Structure-Activity Relationship

Substances

  • Intracellular Signaling Peptides and Proteins
  • Protein Kinase Inhibitors
  • MAP-kinase-activated kinase 2
  • MAP-kinase-activated kinase 3
  • Protein Serine-Threonine Kinases