Solution NMR studies reveal no global flexibility in the catalytic domain of CDC25B.

@article{Lund2014SolutionNS,
  title={Solution NMR studies reveal no global flexibility in the catalytic domain of CDC25B.},
  author={George Lund and Tomasz Cierpicki},
  journal={Proteins},
  year={2014},
  volume={82 11},
  pages={2889-95}
}
The CDC25B phosphatase is a critical regulator of the cell cycle and has been validated as an important therapeutic target in cancer. Previous studies using molecular dynamics simulations have concluded that the catalytic domain of CDC25B may experience a significant degree of dynamics or be partially disordered in solution, a finding that has a pronounced impact on the structure-based development of CDC25B inhibitors. We have probed the backbone dynamics of the CDC25B catalytic domain in… CONTINUE READING
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