Crystal Structure of the Dual Specificity Protein Phosphatase VHR

@article{Yuvaniyama1996CrystalSO,
  title={Crystal Structure of the Dual Specificity Protein Phosphatase VHR},
  author={Jirundon Yuvaniyama and John M. Denu and Jack E. Dixon and Mark A. Saper},
  journal={Science},
  year={1996},
  volume={272},
  pages={1328 - 1331}
}
Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. Here, the crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), was determined at 2.1 angstrom resolution. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine… 
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