Difference between revisions of "Part:BBa K4165093"
 
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===Functional Parameters===
 
===Functional Parameters===
  
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GC Content%
 
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60.9%
 
  
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Isoelectric point (PI)
 
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4.993
 
  
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Charge at pH 7
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-2.188
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  <tr>
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    <th>GC Content%</th>
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    <th>Isoelectric point (PI)</th>
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    <th>Charge at pH 7</th>
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    <th>Molecular Weight (Protein)</th>
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  <tr>
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    <td>60.9%</td>
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    <td>4.993</td>
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    <td>-2.188</td>
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    <td>15.535 kDa</td>
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−
Molecular Weight (Protein)
 
−
15.535 kDa
 
  
 
===Modeling===
 
===Modeling===
  
 
The predicted structure (AlphaFold) is present.
 
The predicted structure (AlphaFold) is present.
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−
 
  
  
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                  Figure 1.: A graphical illustration showing the structure of the inhibitor.
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                          Figure 1.: A graphical illustration showing the structure of the inhibitor.
  
 
===References===
 
===References===

Latest revision as of 11:44, 13 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% Isoelectric point (PI) Charge at pH 7 Molecular Weight (Protein)
60.9% 4.993 -2.188 15.535 kDa


Modeling

The predicted structure (AlphaFold) is present. 


                         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.