@article{215,
  keywords = {Benzamides, Humans, Imatinib Mesylate, Models, Molecular, Orosomucoid, Piperazines, Protein Binding, Protein Conformation, Protein Kinase Inhibitors, Pyrimidines, Spectrum Analysis},
  author = {I Fitos and Á Simon and Ferenc Zsila and G Mády and Á Bencsura and Zoltán Varga and L Orfi and G Kéri and J Visy},
  title = {Characterization of binding mode of imatinib to human α1-acid glycoprotein.},
  abstract = {<p>Imatinib (IMT) is a selective tyrosine kinase inhibitor, used in the treatment of chronic myeloid leukemia and gastrointestinal stromal tumors. Its strong plasma protein binding was found to belong to the F1*S genetic variant of α(1)-acid glycoprotein (AGP). In this work, comparative AGP binding studies were performed with IMT fragment molecules to reveal which parts of the molecule are important in the high-affinity interaction provoking specific spectral changes. Molecular modeling calculations indicated that IMT docked into the X-ray structure of AGP/F1 adopts a bent, compact conformation. This binding mode is similar to those found in its complexes with some low-affinity kinases and a quinone reductase, being strikingly different from the extended conformation of IMT in its high-affinity kinase targets.</p>},
  year = {2012},
  journal = {Int J Biol Macromol},
  volume = {50},
  pages = {788-95},
  month = {2012 Apr 1},
  issn = {1879-0003},
  doi = {10.1016/j.ijbiomac.2011.11.023},
}