An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering

@article{Keedy2018AnEA,
  title={An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering},
  author={Daniel A. Keedy and Zachary B. Hill and Justin T. Biel and Emily Kang and Terry Justin Rettenmaier and Jos{\'e} Brand{\~a}o-Neto and Nicholas M. Pearce and Frank von Delft and James A. Wells and James S. Fraser},
  journal={eLife},
  year={2018},
  volume={7}
}
Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function. Here, we have identified allosteric sites in protein tyrosine phosphatase 1B (PTP1B) by combining multiple-temperature X-ray crystallography experiments and structure determination from hundreds of individual small-molecule fragment soaks. New… 

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