Difference between revisions of "Part:BBa K4165092"
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | This type of inhibitor is predicted to be able to inhibit trypsin-like proteases. This inhibitor plays a major role in male fertility and reproduction. It also provides antimicrobial activity for the sperms. 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[ | + | This type of inhibitor is predicted to be able to inhibit trypsin-like proteases. This inhibitor plays a major role in male fertility and reproduction. It also provides antimicrobial activity for the sperms. 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_K4165092 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4165092 SequenceAndFeatures</partinfo> | ||
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| − | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/13-alphafold.png" style="margin-left:200px;" alt="" width="500" /></p> | + | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/switches/13-alphafold.png" style="margin-left:200px;" alt="" width="500" /></p> |
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===References=== | ===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. | + | 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.<br> |
| − | 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. | + | 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.<br> |
| − | 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. | + | 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.<br> |
<partinfo>BBa_K4165092 parameters</partinfo> | <partinfo>BBa_K4165092 parameters</partinfo> | ||
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Revision as of 19:39, 10 October 2022
EPPIN (epididymal peptidase inhibitor).
This basic part encodes Human serine protease inhibitor epididymal peptidase inhibitor which is predicted to be able to inhibit HtrA1 (BBa_K4165004).
Usage and Biology
This type of inhibitor is predicted to be able to inhibit trypsin-like proteases. This inhibitor plays a major role in male fertility and reproduction. It also provides antimicrobial activity for the sperms. 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
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 303
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 303
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 303
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 303
- 1000COMPATIBLE WITH RFC[1000]
Functional Parameters
GC Content% 61.7%
Isoelectric point (PI) 7.827
Charge at pH 7 4.07
Molecular Weight (Protein) 15.284
PDB Structure
Denovo modelling - AlphaFold2
AlphaFold: https://alphafold.ebi.ac.uk/entry/O95925 Molprobity = 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.