Function
Trypsin inhibitors (TI) inhibit the enzymatic activity of serine proteases and thus have nutritional effect. TI natural sources are bovine, ovomucoid, soybean, lima bean and other plants. See also Basic Pancreatic Trypsin Inhibitor.
Disease
Relevance
Structural highlights
3D Structures of trypsin inhibitor
Updated on 21-August-2014
Trypsin inhibitor
1cti, 2cti, 3cti – sTI - squash - NMR
1lu0, 2v1v – sTI (mutant)
1jbl, 1jbn, 1o8y, 1o8z – suTI – sunflower - NMR
1t9e – suTI (mutant) - NMR
2ab9 – suTI precursor - NMR
Trypsin inhibitor complex with protease
1ppe, 2sta – sTI + trypsin
1sfi, 4hgc – suTI + trypsin
3p8f – suTI + membrane-type serine protease
4k1e, 4kel – suTI (mutant) + kallikrein-4
4k8y – suTI + kallikrein-4
References
