Difference between revisions of "Part:BBa K4165087"
 
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===Functional Parameters===
 
===Functional Parameters===
  
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GC Content%
 
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67.6%
 
  
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Isoelectric point (PI)
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<html>
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5.112
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<style>
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table, th, td {
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  border:1px solid black; margin-left:auto;margin-right:auto;
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}
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<body>
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<table style="width:65%">
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<table>
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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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  <tr>
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    <td>67.6%</td>
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    <td>5.112</td>
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    <td>-3.555</td>
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    <td>12.05 kDa</td>
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  </tr>
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</table>
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</body>
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</html>
  
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Charge at pH 7
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===Modeling===
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-3.555
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−
 
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Molecular Weight (Protein)
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12.05 kDa
+
  
 
The available structure is the predicted one (AlphaFold2).
 
The available structure is the predicted one (AlphaFold2).
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AlphaFold2
 
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https://alphafold.ebi.ac.uk/entry/Q8WWY7
 
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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 =
 
  
  
 
<html>
 
<html>
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/8-alphafold.png" style="margin-left:200px;" alt="" width="500" /></p>
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/switches/8-alphafold.png" style="margin-left:200px;" alt="" width="500" /></p>
 
</html>
 
</html>
  
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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.
  
  
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===References===
 
===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.
+
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. <br>
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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.
+
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. <br>
−
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.
+
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.<br>
  
 
<partinfo>BBa_K4165087 parameters</partinfo>
 
<partinfo>BBa_K4165087 parameters</partinfo>
 
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Latest revision as of 12:13, 13 October 2022


WAP-four disulfide core domain 12 serine protease inhibitor.

This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 12 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 has 8 cysteine residues capable of forming four disulphide 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
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Functional Parameters

GC Content% Isoelectric point (PI) Charge at pH 7 Molecular Weight (Protein)
67.6% 5.112 -3.555 12.05 kDa

Modeling

The available structure is the predicted one (AlphaFold2). 


                     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.