Difference between revisions of "Part:BBa K4165093"
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This basic part encodes Histocompatibility minor serpin domain which is predicted to be able to inhibit HtrA1 (BBa_K4165004).
 
This basic part encodes Histocompatibility minor serpin domain 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 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 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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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<sup>[1-3]</sup>.
  
  
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===<span class='h3bb'>Sequence and Features</span>===
 
===<span class='h3bb'>Sequence and Features</span>===
 
<partinfo>BBa_K4165093 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4165093 SequenceAndFeatures</partinfo>
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===Functional Parameters===
 
===Functional Parameters===
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15.535 kDa
 
15.535 kDa
  
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===PDB Structure===
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===Dry lab===
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<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
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The predicted structure (AlphaFold) is present.
 
The predicted structure (AlphaFold) is present.
  

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


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 400
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 400
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 400
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 400
  • 1000
    COMPATIBLE 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.