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Kunitz domain information


Kunitz/Bovine pancreatic trypsin inhibitor domain
3D structure of the C-terminal Kunitz domain from human collagen alpha-3(VI) chain.[1]
Identifiers
SymbolKunitz_BPTI
PfamPF00014
InterProIPR002223
PROSITEPDOC00252
SCOP25pti / SCOPe / SUPFAM
CDDcd00109
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1knt :3110-3162 2knt :3110-3162 1kthA:3110-3162

1kun :3110-3162 1bik :286-338 1shp :2-54 1jc6A:6-58 1bf0 :6-58 1dtk :26-78 1dtx :6-58 1den :6-58 1dem :6-58 1zr0D:35-87 1irhA:216-268 1adz :124-176 1tfxC:124-176 1d0dB:39-91 1k6uA:39-91 2fi4I:39-91 1aalA:39-91 2kaiI:39-91 1ejmD:39-91 1fakI:39-90 1bhcG:39-91 2hexC:39-91 1bthQ:39-91 3btwI:39-91 1p2qB:39-91 1bz5C:39-91 3bthI:39-91 1oa65:39-91 1eawB:39-91 3btmI:39-91 1oa55:39-91 2tpiI:39-91 1pit :39-91 3btdI:39-91 1b0cD:39-91 3btfI:39-91 1t8mB:39-91 1ld5A:39-91 1bzxI:39-91 1p2jI:39-91 1uubA:39-91 3tgkI:39-91 1t7cD:39-91 1tpaI:39-91 1p2nB:39-91 1p2kI:39-91 1t8nB:39-91 1g6xA:39-91 1nag :39-91 8pti :39-91 2fi3I:39-91 1t8oB:39-91 1k09B:50-73 1p2mB:39-91 6pti :39-91 3tpiI:39-91 1t8lD:39-91 3btgI:39-91 3tgjI:39-91 1brbI:42-90 1jv9A:39-91 1f7zI:39-91 1fy8I:39-91 2ptcI:39-91 2tgpI:39-91 1mtnD:39-91 1cbwI:39-91 1jv8A:39-91 1f5rI:39-91 7pti :39-91 3bteI:39-91 1fan :39-91 3tgiI:39-91 3btkI:39-91 5pti :39-91 1uuaA:39-91 9pti :39-91 3bttI:39-91 1bpi :39-91 1p2oD:39-91 1bpt :39-91 1p2iI:39-91 4pti :39-91 1qlqA:39-91 1ld6A:39-91 3btqI:39-91 4tpiI:39-91 1bti :39-91 1yc0I:249-301 1ca0I:290-342 1aapB:290-342 1tawB:290-342 1brcI:290-342 1zjdB:290-342 1bunB:30-82 1tocR:4-51

1kigI:4-60 1tap :4-60 1tcp :4-60

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]

  1. ^ 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.
  2. ^ Nixon, AE; Wood, CR (2006). "Engineered protein inhibitors of proteases". Current Opinion in Drug Discovery & Development. 9 (2): 261–8. PMID 16566296.

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amino-terminus, three tandemly linked Kunitz domains, and a highly positively charged carboxy-terminus. With its Kunitz domains, TFPI exhibits significant homology...

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kallikrein and a 60-amino acid polypeptide which was developed from a Kunitz domain through phage display to mimic antibodies inhibiting kallikrein. On...

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consist of a high variety of putative toxins, including ShKT domain- and Kunitz domain- containing proteins which are potential therapeutic compounds...

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carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2". Biochemistry. 35 (20): 6450–9. doi:10...

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signal peptide, a WAP domain, a follistatin domain, an immunoglobulin domain, two tandem Kunitz domains, and an NTR domain. These domains have been implicated...

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such as scorpions, snakes, spiders, and sea anemones. All Kunitz peptides share the Kunitz domain, which is characterized by a peptide chain of approximately...

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SPINT2 gene. SPINT2 is a transmembrane protein with two extracellular Kunitz domains to inhibit serine proteases. This gene is a presumed tumor suppressor...

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WFIKKN2

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follistatin domain, immunoglobulin domain, two tandem Kunitz domains, and an NTR domain. This gene encodes a WFIKKN1-related protein which has the same domain organization...

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protein. The extracellular domain (residues 32-692) contains the E1 domain, E2 domain, and BPTI/Kunitz inhibitor domain. The E1 domain contains two independent...

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