Difference between revisions of "Part:BBa K4165092"

 
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<partinfo>BBa_K4165092 short</partinfo>
 
<partinfo>BBa_K4165092 short</partinfo>
  
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A serine protease inhibitor is used to inhibit the action of HTRA1
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This basic part encodes Human serine protease inhibitor epididymal peptidase inhibitor which is predicted to be able to inhibit HtrA1 (BBa_K4165004).
  
  
  
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===Usage and Biology===
 
===Usage and Biology===
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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].
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===Functional Parameters===
 
===Functional Parameters===
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GC Content%
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61.7%
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Isoelectric point (PI)
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7.827
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Charge at pH 7
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4.07
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Molecular Weight (Protein)
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15.284
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===PDB Structure===
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Denovo modelling - AlphaFold2
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AlphaFold:
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https://alphafold.ebi.ac.uk/entry/O95925
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Molprobity =
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Q_Mean =
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Ramachandran Favoured =
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Ramachandran Outliers =
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Clash Score =
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C-beta Deviation =
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Rotamers outliers =
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Total Score =
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===References===
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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.
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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.
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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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<partinfo>BBa_K4165092 parameters</partinfo>
 
<partinfo>BBa_K4165092 parameters</partinfo>
 
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Revision as of 19:01, 5 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[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 =



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.