Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3  

@article{Ng2000StructuralBF,
  title={Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3  },
  author={K. Ng and J. Petersen and M. Cherney and C. Garen and Jeffrey J Zalatoris and C. Rao-Naik and B. Dunn and M. Martzen and R. Peanasky and M. James},
  journal={Nature Structural Biology},
  year={2000},
  volume={7},
  pages={653-657}
}
The three-dimensional structures of pepsin inhibitor-3 (PI-3) from Ascaris suum and of the complex between PI-3 and porcine pepsin at 1.75 Å and 2.45 Å resolution, respectively, have revealed the mechanism of aspartic protease inhibition by this unique inhibitor. PI-3 has a new fold consisting of two domains, each comprising an antiparallel β-sheet flanked by an α-helix. In the enzyme–inhibitor complex, the N-terminal β-strand of PI-3 pairs with one strand of the ‘active site flap’ (residues 70… Expand
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