| Kunitz/Bovine pancreatic trypsin inhibitor domain | |||||||||||
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| Identifiers | |||||||||||
| Symbol | Kunitz_BPTI | ||||||||||
| Pfam | PF00014 | ||||||||||
| InterPro | IPR002223 | ||||||||||
| PROSITE | PDOC00252 | ||||||||||
| SCOP2 | 5pti / SCOPe / SUPFAM | ||||||||||
| CDD | cd00109 | ||||||||||
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Kunitz domains are the active domains of proteins that inhibit the function of protein degrading enzymes or, more specifically, domains of Kunitz-type are protease inhibitors. They are relatively small with a length of about 50 to 60 amino acids and a molecular weight of 6 kDa. Examples of Kunitz-type protease inhibitors are aprotinin (bovine pancreatic trypsin inhibitor, BPTI), Alzheimer's amyloid precursor protein (APP), and tissue factor pathway inhibitor (TFPI). Kunitz STI protease inhibitor, the trypsin inhibitor initially studied by Moses Kunitz, was extracted from soybeans.
Standalone Kunitz domains are used as a framework for the development of new pharmaceutical drugs.[2]
- ^ PDB: 1KTH; Arnoux B, Ducruix A, Prangé T (July 2002). "Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 Å)". Acta Crystallogr. D. 58 (Pt 7): 1252–4. doi:10.1107/S0907444902007333. PMID 12077460.
- ^ Nixon, AE; Wood, CR (2006). "Engineered protein inhibitors of proteases". Current Opinion in Drug Discovery & Development. 9 (2): 261–8. PMID 16566296.