Difference between revisions of "Part:BBa K4165093"
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| − | Q_Mean = | + | Q_Mean = |
| − | Ramachandran Favoured = | + | Ramachandran Favoured = |
| − | Ramachandran Outliers = | + | Ramachandran Outliers = |
| − | Clash Score = | + | Clash Score = |
| − | C-beta Deviation = | + | C-beta Deviation = |
| − | Rotamers outliers = | + | Rotamers outliers = |
| − | Total Score = | + | Total Score = |
Revision as of 23:08, 11 October 2022
Histocompatibility minor serpin domain (HMSD).
This basic part encodes Histocompatibility minor serpin domain which is predicted to be able to inhibit HtrA1 (BBa_K4165004).
Usage and Biology
This gene encodes a protein with a serpin domain that may act as a serine protease inhibitor. This gene is predominantly expressed in myeloid cells. A splice variant encoding a minor histocompatibility antigen may be expressed as a result of a polymorphism in this gene. This type of inhibitor is predicted to have a 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
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 400
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 400
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 400
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 400
- 1000COMPATIBLE WITH RFC[1000]
Functional Parameters
GC Content% 60.9%
Isoelectric point (PI) 4.993
Charge at pH 7 -2.188
Molecular Weight (Protein) 15.535 kDa
Dry lab
Modeling
The predicted structure (AlphaFold) is present.
AlphaFold https://alphafold.ebi.ac.uk/entry/A8MTL9
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.