Difference between revisions of "Part:BBa K4165090"
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| + | Figure 1.: A graphical illustration showing the structure of the inhibitor. | ||
===References=== | ===References=== | ||
Revision as of 14:49, 6 October 2022
WAP-four disulfide core domain 6 serine protease inhibitor.
This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 6 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 has 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 252
- 1000COMPATIBLE WITH RFC[1000]
Functional Parameters
GC Content% 63.6%
Isoelectric point (PI) 7.981
Charge at pH 7 4.57
Molecular Weight (Protein) 14.626 kDa
PDB Structures
The predicted structure (AlphaFold2) is presented.
AlphaFold2 https://alphafold.ebi.ac.uk/entry/Q9BQY6 Q_Mean = Ramachandran Favoured = Ramachandran Outliers = Clash Score = C-beta Deviation = Rotamers outliers = Total Score =
Figure 1.: A graphical illustration showing the structure of the inhibitor.
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.