Role of ELA region in auto-activation of mutant KIT receptor: a molecular dynamics simulation insight

@article{Purohit2014RoleOE,
  title={Role of ELA region in auto-activation of mutant KIT receptor: a molecular dynamics simulation insight},
  author={R. Purohit},
  journal={Journal of Biomolecular Structure and Dynamics},
  year={2014},
  volume={32},
  pages={1033 - 1046}
}
  • R. Purohit
  • Published 2014
  • Medicine, Chemistry
  • Journal of Biomolecular Structure and Dynamics
  • KIT receptor is the prime target in gastrointestinal stromal tumor (GISTs) therapy. Second generation inhibitor, Sunitinib, binds to an inactivated conformation of KIT receptor and stabilizes it in order to prevent tumor formation. Here, we investigated the dynamic behavior of wild type and mutant D816H KIT receptor, and emphasized the extended A-loop (EAL) region (805–850) by conducting molecular dynamics simulation (∼100 ns). We analyzed different properties such as root mean square cutoff or… CONTINUE READING
    90 Citations
    Impact of point mutation P29S in RAC1 on tumorigenesis
    • 45
    Unraveling the molecular effects of mutation L270P on Wiskkot–Aldrich syndrome protein: insights from molecular dynamics approach
    • 4
    Deciphering the Molecular Effects of Mutations on ATRX Cause ATRX Syndrome: A Molecular Dynamics Study
    • 3

    References

    SHOWING 1-10 OF 52 REFERENCES
    Drug binding and resistance mechanism of KIT tyrosine kinase revealed by hydrogen/deuterium exchange FTICR mass spectrometry
    • 25
    KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients
    • 289
    • Highly Influential
    • PDF
    Structural Basis for the Autoinhibition and STI-571 Inhibition of c-Kit Tyrosine Kinase*
    • 530
    • Highly Influential
    • PDF
    In silico investigation of molecular mechanism of laminopathy caused by a point mutation (R482W) in lamin A/C protein
    • 121
    Structural basis for the resilience of Darunavir (TMC114) resistance major flap mutations of HIV-1 protease
    • 45
    Studies on Adaptability of Binding Residues Flap Region of TMC-114 Resistance HIV-1 Protease Mutants
    • 61