Conformational Selection and Induced Fit Mechanisms in the Binding of an Anticancer Drug to the c-Src Kinase

@inproceedings{Morando2016ConformationalSA,
  title={Conformational Selection and Induced Fit Mechanisms in the Binding of an Anticancer Drug to the c-Src Kinase},
  author={Mar{\'i}a Agnese Morando and Giorgio Saladino and Nicola D’Amelio and Encarna Pucheta-Martinez and Silvia Lovera and Moreno Lelli and Blanca L{\'o}pez-M{\'e}ndez and Marco Marenchino and Ram{\'o}n Campos-Olivas and Francesco Luigi Gervasio},
  booktitle={Scientific reports},
  year={2016}
}
Understanding the conformational changes associated with the binding of small ligands to their biological targets is a fascinating and meaningful question in chemistry, biology and drug discovery. One of the most studied and important is the so-called "DFG-flip" of tyrosine kinases. The conserved three amino-acid DFG motif undergoes an "in to out" movement resulting in a particular inactive conformation to which "type II" kinase inhibitors, such as the anti-cancer drug Imatinib, bind. Despite… CONTINUE READING
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SHOWING 1-10 OF 59 REFERENCES

Structural and dynamic insights into the energetics of activation loop rearrangement in FGFR1 kinase

T Klein
  • Nat. Commun
  • 2015

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2013

Molecular Mechanism of SSR128129E, an Extracellularly Acting, Small-Molecule, Allosteric Inhibitor of FGF Receptor Signaling

C Herbert
  • Cancer Cell 23,
  • 2013

Transitions to catalytically inactive conformations in EGFR kinase.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2013