Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors

J Biol Chem. 1992 Jan 25;267(3):1990-4. doi: 10.2210/pdb1pi2/pdb.

Abstract

The three-dimensional structure of the Bowman-Birk type proteinase inhibitor (PI-II) has been determined by x-ray crystallography and refined at 2.5-A resolution. This protein is a specific inhibitor of trypsin. Two reactive site loops, one at each end of the PI-II molecule, are structurally similar to each other and to reactive-site loops of pancreatic secretory trypsin inhibitor (Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos, E., and Huber, R. (1982) J. Mol. Biol. 162, 839-869) and bovine pancreatic trypsin inhibitor (Deisenhofer, J., and Steigemann, W. (1975) Acta Crystallogr. B31, 238-250). PI-II is the first reported Bowman-Birk type inhibitor structure to be refined at high resolution, providing further insight into inhibitor mechanisms.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antineoplastic Agents / chemistry*
  • Binding Sites
  • Models, Molecular
  • Protein Conformation
  • Trypsin Inhibitor, Bowman-Birk Soybean / chemistry*
  • Trypsin Inhibitors / chemistry*
  • X-Ray Diffraction

Substances

  • Antineoplastic Agents
  • Trypsin Inhibitor, Bowman-Birk Soybean
  • Trypsin Inhibitors