Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.
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.
Chen
P
P
Department of Crystallography, University of Pittsburgh, Pennsylvania 15260.
Rose
J
J
Love
R
R
Wei
C H
CH
Wang
B C
BC
D000595:Amino Acid Sequence; D000970:Antineoplastic Agents / Q000737:chemistry*; D001665:Binding Sites; D008958:Models, Molecular; D011487:Protein Conformation; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000737:chemistry*; D014361:Trypsin Inhibitors / Q000737:chemistry*; D014961:X-Ray Diffraction
D000970:Antineoplastic Agents; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D014361:Trypsin Inhibitors