Part:BBa_K4165008
WAP-four disulfide core domain 13 serine protease inhibitor.
This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 13 which is able to inhibit HtrA1 (BBa_K4165004).
Usage and Biology
This type of family encodes for a type of inhibitor that contains a motif which consists of 8 cysteine residues capable of forming four disulfide bonds at the core of the protease, thus inhibiting its action. This type of inhibitor is very effective and has high affinity for trypsin-like proteases (serine proteases), and in our case it would act as an inhibitor for the trypsin-like catalytic domain of serine protease HtrA1[1]-[3].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 270
Illegal AgeI site found at 6 - 1000COMPATIBLE WITH RFC[1000]
Functional Parameters
Isoelectric point (PI) 7.763
Charge at pH 7 2.506
Molecular Weight (Protein) 10.386 kDa
PDB Structure
Homology and denovo modelling - (TRrosetta - AlphaFold2 - RosettaFold - Modeller)
Structure assessment results
Q_Mean =
Ramachandran Favoured =
Ramachandran Outliers =
Clash Score =
C-beta Deviation =
Total Score =
References
1. Clauss, A., Lilja, H., & Lundwall, Å. (2005). The evolution of a genetic locus encoding small serine proteinase inhibitors. Biochemical and biophysical research communications, 333(2), 383-389. 2. Eigenbrot, C., Ultsch, M., Lipari, M. T., Moran, P., Lin, S. J., Ganesan, R., ... & Kirchhofer, D. (2012). Structural and functional analysis of HtrA1 and its subdomains. Structure, 20(6), 1040-1050. 3. Grau, S., Baldi, A., Bussani, R., Tian, X., Stefanescu, R., Przybylski, M., ... & Ehrmann, M. (2005). Implications of the serine protease HtrA1 in amyloid precursor protein processing. Proceedings of the National Academy of Sciences, 102(17), 6021-6026.
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