Difference between revisions of "Part:BBa K4165089"

 
 
(5 intermediate revisions by 4 users not shown)
Line 3: Line 3:
 
<partinfo>BBa_K4165089 short</partinfo>
 
<partinfo>BBa_K4165089 short</partinfo>
  
−
A serine protease inhibitor is used to inhibit the action of HTRA1
+
This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 2 which is able to inhibit HtrA1 (BBa_K4165004).
  
  
−
 
−
<!-- Add more about the biology of this part here
 
 
===Usage and Biology===
 
===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. The main function of this inhibitor is to pervent elastase-mediated tissue proteolysis. 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<sup>[1-3]</sup>.
 +
  
 
<!-- -->
 
<!-- -->
−
<span class='h3bb'>Sequence and Features</span>
+
===<span class='h3bb'>Sequence and Features</span>===
 
<partinfo>BBa_K4165089 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4165089 SequenceAndFeatures</partinfo>
  
  
−
<!-- Uncomment this to enable Functional Parameter display
+
 
 
===Functional Parameters===
 
===Functional Parameters===
 +
 +
 +
<html>
 +
<style>
 +
table, th, td {
 +
  border:1px solid black; margin-left:auto;margin-right:auto;
 +
}
 +
</style>
 +
<body>
 +
<table style="width:65%">
 +
<table>
 +
  <tr>
 +
    <th>GC Content%</th>
 +
    <th>Isoelectric point (PI)</th>
 +
    <th>Charge at pH 7</th>
 +
    <th>Molecular Weight (Protein)</th>
 +
  </tr>
 +
  <tr>
 +
    <td>68.8%</td>
 +
    <td>4.371</td>
 +
    <td>-4.23</td>
 +
    <td>12.993 kDa</td>
 +
  </tr>
 +
</table>
 +
</body>
 +
</html>
 +
 +
 +
===PDB structure===
 +
The predicted structure (AlphaFold2) is presented.
 +
 +
 +
<html>
 +
<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/switches/10-alphafold.png" style="margin-left:200px;" alt="" width="500" /></p>
 +
</html>
 +
 +
                  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. <br>
 +
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.<br>
 +
 +
 
<partinfo>BBa_K4165089 parameters</partinfo>
 
<partinfo>BBa_K4165089 parameters</partinfo>
 
<!-- -->
 
<!-- -->

Latest revision as of 12:10, 13 October 2022


WAP-four disulfide core domain 2 serine protease inhibitor.

This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 2 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. The main function of this inhibitor is to pervent elastase-mediated tissue proteolysis. 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
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 115
    Illegal PstI site found at 183
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 115
    Illegal PstI site found at 183
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 115
    Illegal PstI site found at 183
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 115
    Illegal PstI site found at 183
    Illegal NgoMIV site found at 3
  • 1000
    COMPATIBLE WITH RFC[1000]


Functional Parameters

GC Content% Isoelectric point (PI) Charge at pH 7 Molecular Weight (Protein)
68.8% 4.371 -4.23 12.993 kDa


PDB structure

The predicted structure (AlphaFold2) is presented. 


                 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.