High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site.

@article{Grasberger1994HighresolutionSO,
  title={High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site.},
  author={Bruce L Grasberger and G Marius Clore and Angela M. Gronenborn},
  journal={Structure},
  year={1994},
  volume={2 7},
  pages={669-78}
}
BACKGROUND The Ascaris trypsin inhibitor (ATI) is a member of a new family of serine protease inhibitors isolated from the helminthic worm Ascaris lumbricoides var suum. This family comprises five chymotrypsin/elastase inhibitors and one trypsin inhibitor. Members are characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. RESULTS The solution structure of ATI has been determined… CONTINUE READING

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