1PI2

REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS

Summary for 1PI2

• Entry DOI: 10.2210/pdb1pi2/pdb
• Descriptor: BOWMAN-BIRK INHIBITOR (PI-II) (1 entity in total)
• Functional Keywords: serine proteinase inhibitor
• Biological source: Glycine max (soybean)
• Total number of polymer chains: 1
• Total formula weight: 7213.34

Authors

Chen, P.,Rose, J.,Wang, B.C. (deposition date: 1991-03-26, release date: 1992-04-15, Last modification date: 2024-10-09)

Primary citation

Chen, P.,Rose, J.,Love, R.,Wei, C.H.,Wang, B.C.
Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.
J.Biol.Chem., 267:1990-1994, 1992

PubMed 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.

PubMed: 1730730

Experimental method

X-RAY DIFFRACTION (2.5 Å)