1pi2
REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS
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OverviewOverview
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.
About this StructureAbout this Structure
1PI2 is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
ReferenceReference
Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors., Chen P, Rose J, Love R, Wei CH, Wang BC, J Biol Chem. 1992 Jan 25;267(3):1990-4. PMID:1730730
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