Coding

Part:BBa_K4165092

Designed by: Mennatallah Mahmoud Mohamed Abdelzaher Turky   Group: iGEM22_CU_Egypt   (2022-09-30)
Revision as of 14:58, 6 October 2022 by Ahmedsameh (Talk | contribs) (→‎PDB Structure)


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[7]-[9].


Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 303
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 303
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 303
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 303
  • 1000
    COMPATIBLE 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.


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