Structure of a serpin–protease complex shows inhibition by deformation

@article{Huntington2000StructureOA,
  title={Structure of a serpin–protease complex shows inhibition by deformation},
  author={James A. Huntington and Randy J Read and Robin W. Carrell},
  journal={Nature},
  year={2000},
  volume={407},
  pages={923-926}
}
The serpins have evolved to be the predominant family of serine-protease inhibitors in man. Their unique mechanism of inhibition involves a profound change in conformation, although the nature and significance of this change has been controversial. Here we report the crystallographic structure of a typical serpin–protease complex and show the mechanism of inhibition. The conformational change is initiated by reaction of the active serine of the protease with the reactive centre of the serpin… CONTINUE READING
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