Molecular dynamics studies on the interactions of PTP1B with inhibitors: from the first phosphate-binding site to the second one.

  title={Molecular dynamics studies on the interactions of PTP1B with inhibitors: from the first phosphate-binding site to the second one.},
  author={Jingfang Wang and Ke Gong and Dongqing Wei and Yixue Li and Kuo-Chen Chou},
  journal={Protein engineering, design \& selection : PEDS},
  volume={22 6},
Protein tyrosine phosphatases 1B (PTP1B) is a major negative regulator of both insulin and leptin signaling pathways. In view of this, it becomes an important target for drug development against cancers, diabetes and obesity. The aim of the current study is to use the long time-scale molecular dynamics (MD) simulations to investigate the structural and dynamic factors that cause its inhibition by INTA and INTB, the two most potent and highly selective PTP1B inhibitors known so far. In order to… 

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