Trypsin inhibitor

From Proteopedia

spinqualitylabelsall models Squash seed trypsin inhibitor structure (deepskyblue) complex with trypsin (magenta) and Ca+2 ion (green) (PDB code 2sta). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 3D Structures of trypsin inhibitor 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. Kunitz-type TI are found in legume seeds[1]. Kunitz-type miraculin-like proteins are part of the soybean TI [2]. Bowman-Birk-type TI are found in legume and cereal grains seeds[3]. See also Basic Pancreatic Trypsin Inhibitor. Relevance The TI ulinastatin is used for the initial treatment of Kawasaki disease[4]. Structural highlights The [5]. Water molecules are shown as red spheres. . 3D Structures of trypsin inhibitor Trypsin inhibitor 3D structures

References

1. ↑ Song HK, Suh SW. Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. J Mol Biol. 1998 Jan 16;275(2):347-63. PMID:9466914 doi:10.1006/jmbi.1997.1469
2. ↑ Ohkura SI, Hori M, Saitoh K, Okuzawa T, Okamoto I, Furukawa N, Shimizu-Ibuka A. Structural and functional analysis of miraculin-like protein from Vitis vinifera. Biochim Biophys Acta Proteins Proteom. 2018 Nov;1866(11):1125-1130. doi:, 10.1016/j.bbapap.2018.08.009. Epub 2018 Aug 27. PMID:30282610 doi:http://dx.doi.org/10.1016/j.bbapap.2018.08.009
3. ↑ Liener IE, Goodale RL, Deshmukh A, Satterberg TL, Ward G, DiPietro CM, Bankey PE, Borner JW. Effect of a trypsin inhibitor from soybeans (Bowman-Birk) on the secretory activity of the human pancreas. Gastroenterology. 1988 Feb;94(2):419-27. PMID:2446949
4. ↑ Kanai T, Ishiwata T, Kobayashi T, Sato H, Takizawa M, Kawamura Y, Tsujimoto H, Nakatani K, Ishibashi N, Nishiyama M, Hatai Y, Asano Y, Kobayashi T, Takeshita S, Nonoyama S. Ulinastatin, a urinary trypsin inhibitor, for the initial treatment of patients with Kawasaki disease: a retrospective study. Circulation. 2011 Dec 20;124(25):2822-8. doi: 10.1161/CIRCULATIONAHA.111.028423. , Epub 2011 Nov 21. PMID:22104548 doi:http://dx.doi.org/10.1161/CIRCULATIONAHA.111.028423
5. ↑ Helland R, Berglund GI, Otlewski J, Apostoluk W, Andersen OA, Willassen NP, Smalas AO. High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes. Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):139-48. Epub 1999, Jan 1. PMID:10089404 doi:10.1107/S090744499801052X