Difference between revisions of "Part:BBa K4165008"

 
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This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 13 which is able to inhibit HtrA1 (BBa_K4165004).
 
This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 13 which is able to inhibit HtrA1 (BBa_K4165004).
  
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===Usage and Biology===
 
===Usage and Biology===
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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. 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].
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===Functional Parameters===
 
===Functional Parameters===
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Isoelectric point (PI)
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7.763
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Charge at pH 7
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2.506
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Molecular Weight (Protein)
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10.386 kDa
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===PDB Structure===
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Homology and denovo modelling - (TRrosetta - AlphaFold2 - RosettaFold - Modeller)
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Structure assessment results
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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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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_K4165008 parameters</partinfo>
 
<partinfo>BBa_K4165008 parameters</partinfo>
 
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Revision as of 19:35, 5 October 2022


WAP-four disulfide core domain 13 serine protease inhibitor.

This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 13 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. 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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 270
    Illegal AgeI site found at 6
  • 1000
    COMPATIBLE WITH RFC[1000]


Functional Parameters

Isoelectric point (PI) 7.763

Charge at pH 7 2.506

Molecular Weight (Protein) 10.386 kDa

PDB Structure

Homology and denovo modelling - (TRrosetta - AlphaFold2 - RosettaFold - Modeller)


Structure assessment results Q_Mean = Ramachandran Favoured = Ramachandran Outliers = Clash Score = C-beta Deviation = 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.