Publication | Open Access
Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.
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References
1992
Year
X-ray CrystallographyReactive SitesPathologyMolecular BiologyReactive-site LoopsProtein FoldingAnti-cancer AgentProteomicsSecretory PathwayMulti-protein AssemblyInhibitory ActivityCancer ResearchOther Trypsin InhibitorsProtein FunctionBiochemistryOncogenic AgentThree-dimensional StructurePharmacologyStructural BiologyNatural SciencesMedicineDrug Discovery
The three-dimensional structure of the Bowman-Birk type proteinase inhibitor (PI-11) has been deter; mined by x-ray crystallography and refined at 2.6-A resolution.This protein is a specific inhibitor of trypsin.Two reactive site loops, one at each end of the PI-I1 molecule, are structurally similar to each other and to reactive-site loops of pancreatic secretory trypsin inhibitor (Bolognesi, M.,
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