Difference between revisions of "Part:BBa K4165088"
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===Usage and Biology=== | ===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. The main function of this inhibitor is to prevent elastase-mediated tissue proteolysis. 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 | + | 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. The main function of this inhibitor is to prevent elastase-mediated tissue proteolysis. 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<sup>[1-3]</sup>. |
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| − | <span class='h3bb'>Sequence and Features</span> | + | ===<span class='h3bb'>Sequence and Features</span>=== |
<partinfo>BBa_K4165088 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4165088 SequenceAndFeatures</partinfo> | ||
Revision as of 19:26, 10 October 2022
WAP-four disulfide core domain 14 serine protease inhibitor.
This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 14 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. The main function of this inhibitor is to prevent elastase-mediated tissue proteolysis. 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]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 132
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 189
- 1000COMPATIBLE WITH RFC[1000]
Functional Parameters
GC Content% 67.5%
Isoelectric point (PI) 8.641
Charge at pH 7 6.373
Molecular Weight (Protein) 12.27 kDa
PDB structure
X-ray, NMR, and the predicted structures (AlphaFold2) are all present.
X-ray https://www.rcsb.org/structure/1FLE Q_Mean = Ramachandran Favoured = Ramachandran Outliers = Clash Score = C-beta Deviation = Rotamers outliers = Total Score =
NMR: https://www.rcsb.org/structure/2REL Q_Mean = Ramachandran Favoured = Ramachandran Outliers = Clash Score = C-beta Deviation = Rotamers outliers = Total Score =
AlphaFold https://alphafold.ebi.ac.uk/entry/P19957 Q_Mean = Ramachandran Favoured = Ramachandran Outliers = Clash Score = C-beta Deviation = Rotamers outliers = Total Score =
Figure 1.: A graphical illustration showing the domains of TRIM21.
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.