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Publication Detail
Mechanism of drug efficacy within the EGF receptor revealed by microsecond molecular dynamics simulation.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Wan S, Wright DW, Coveney PV
  • Publication date:
  • Pagination:
    2394, 2400
  • Journal:
    Mol Cancer Ther
  • Volume:
  • Issue:
  • Status:
  • Country:
    United States
  • PII:
  • Language:
  • Keywords:
    Adenosine Triphosphate, Antineoplastic Agents, Binding Sites, Enzyme Stability, Humans, Hydrophobic and Hydrophilic Interactions, Ligands, Molecular Dynamics Simulation, Mutant Proteins, Mutation, Principal Component Analysis, Protein Binding, Protein Kinase Inhibitors, Protein Structure, Secondary, Protein Structure, Tertiary, Quinazolines, Receptor, Epidermal Growth Factor, Time Factors
The EGF receptor (EGFR) regulates important cellular processes including proliferation, differentiation, and apoptosis. EGFR is frequently overexpressed in a range of cancers and is associated with disease progression and treatment. Clinical studies have shown that EGFR mutations confer tumor sensitivity to tyrosine kinase inhibitors in patients with non-small cell lung cancer. In this study, we have conducted molecular dynamics simulations over several microseconds for wild-type and L858R mutant forms of EGFR in the ligand-free state. Close inspection of the conformations and interactions within the binding pocket reveals, converse to the wild type, that the mutant EGFR prefers to bind gefitinib, a targeted anticancer drug, rather than ATP, offering an explanation for why gefitinib is more effective in patients with EGFR mutations than those without.
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