Pancreatic trypsin inhibitor Kunitz domain
Short name | Kunitz_BPTI |
Overlapping homologous superfamilies |
Description
+-----------------------+ | +--------+ | | | **|******* | xxCxxC#xxxCxxxCxxxxxxCxxxxCxx | | +----------+ {------50 residues------} 'C': conserved cysteine involved in a disulfide bond. '#': active site residue. '*': position of the pattern.
References
1.Crystal structure of a Y35G mutant of bovine pancreatic trypsin inhibitor. Housset D, Kim KS, Fuchs J, Woodward C, Wlodawer A. J. Mol. Biol. 220, 757-70, (1991). View articlePMID: 1714504
2.Inter-alpha-trypsin inhibitor: emergence of a family within the Kunitz-type protease inhibitor superfamily. Salier JP. Trends Biochem. Sci. 15, 435-9, (1990). View articlePMID: 1703675
3.Evolutionary origin of a Kunitz-type trypsin inhibitor domain inserted in the amyloid beta precursor protein of Alzheimer's disease. Ikeo K, Takahashi K, Gojobori T. J. Mol. Evol. 34, 536-43, (1992). View articlePMID: 1593645
4.Molecular cloning, expression, and partial characterization of a second human tissue-factor-pathway inhibitor. Sprecher CA, Kisiel W, Mathewes S, Foster DC. Proc. Natl. Acad. Sci. U.S.A. 91, 3353-7, (1994). View articlePMID: 8159751
5.Amino acid sequence of a protease inhibitor isolated from Sarcophaga bullata determined by mass spectrometry. Papayannopoulos IA, Biemann K. Protein Sci. 1, 278-88, (1992). View articlePMID: 1304909
6.Evolutionary families of peptidase inhibitors. Rawlings ND, Tolle DP, Barrett AJ. Biochem. J. 378, 705-16, (2004). View articlePMID: 14705960
7.Protein inhibitors of proteinases. Laskowski M Jr, Kato I. Annu. Rev. Biochem. 49, 593-626, (1980). View articlePMID: 6996568
GO terms
biological process
- None
molecular function
cellular component
- None