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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | The majority of the sequences having this domain belong to the MEROPS inhibitor family I2, clan IB; the Kunitz/bovine pancreatic trypsin inhibitor family, they inhibit proteases of the S1 family [ ] and are restricted to the metazoa with a single exception: Amsacta moorei entomopoxvirus. They are short (~50 residue) α/β proteins with few secondary structures. The fold is constrained by 3 disulphide bonds. The type example for this family is aprotinin (bovine pancreatic trypsin inhibitor) [] (or basic protease inhibitor), but the family includes numerous other members [, , , ], such as snake venom basic protease; mammalian inter-alpha-trypsin inhibitors; trypstatin, a rodent mast cell inhibitor of trypsin; a domain found in an alternatively-spliced form of Alzheimer's amyloid beta-protein; domains at the C-termini of the alpha(1) and alpha(3) chains of type VII and type VI collagens; and tissue factor pathway inhibitor precursor.The pancreatic trypsin inhibitor (Kunitz) family [ , , ] is one of the numerous families of serine proteinase inhibitors. The basic structure of such a type of inhibitor is shown in the following schematic representation:+-----------------------+ | +--------+ || | **|******* | xxCxxC#xxxCxxxCxxxxxxCxxxxCxx| | +----------+{------50 residues------} 'C': conserved cysteine involved in a disulfide bond.'#': active site residue. '*': position of the pattern. | Name | Pancreatic trypsin inhibitor Kunitz domain superfamily |
| Short Name | Kunitz_BPTI_sf | Type | Homologous_superfamily |
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