Structural insight into maternal embryonic leucine zipper kinase (MELK) conformation and inhibition toward structure-based drug design

Biochemistry. 2013 Sep 17;52(37):6380-7. doi: 10.1021/bi4005864. Epub 2013 Sep 4.

Abstract

Maternal embryonic leucine zipper kinase (MELK) is upregulated in several types of tumor, including breast, prostate, and brain tumors. Its expression is generally associated with cell survival, cell proliferation, and resistance to apoptosis. Therefore, the potential of MELK inhibitors as therapeutic agents is recently attracting considerable interest. Here we report the first structures of MELK in complex with AMP-PNP and with nanomolar inhibitors. Our studies shed light on the role of the MELK UBA domain, provide a characterization of the kinase active site, and identify key residues for achieving high potency, laying the groundwork for structure-based drug design efforts.

MeSH terms

  • Adenylyl Imidodiphosphate / pharmacology
  • Antineoplastic Agents / chemistry*
  • Antineoplastic Agents / pharmacology
  • Catalytic Domain
  • Cell Line, Tumor
  • Drug Design
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology
  • High-Throughput Screening Assays
  • Humans
  • Protein Serine-Threonine Kinases / antagonists & inhibitors*
  • Protein Serine-Threonine Kinases / chemistry*
  • Pyrazoles / chemistry
  • Pyrazoles / pharmacology

Substances

  • Antineoplastic Agents
  • Enzyme Inhibitors
  • Pyrazoles
  • Adenylyl Imidodiphosphate
  • MELK protein, human
  • Protein Serine-Threonine Kinases

Associated data

  • PDB/4BKY
  • PDB/4BKZ
  • PDB/4BL1