Difference between revisions of "Part:BBa K4165091"

 
 
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<partinfo>BBa_K4165091 short</partinfo>
 
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A serine protease inhibitor is used to inhibit the action of HTRA1
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This basic part encodes Human serine protease inhibitor secretory leukocyte peptidase inhibitor which is predicted to be able to inhibit HtrA1 (BBa_K4165004).
  
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<!-- Add more about the biology of this part here
 
 
===Usage and Biology===
 
===Usage and Biology===
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This type of inhibitor is considered to be an acid stable inhibitor with very high affinity for trypsins, chymotrypsine, elastases, and cathepsin G <sup>[1-6] </sup>. 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>[7-9] </sup>.
  
 
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<span class='h3bb'>Sequence and Features</span>
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===<span class='h3bb'>Sequence and Features</span>===
 
<partinfo>BBa_K4165091 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4165091 SequenceAndFeatures</partinfo>
  
  
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===Functional Parameters===
 
===Functional Parameters===
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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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<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>67.2%</td>
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    <td>8.494</td>
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    <td>10.831</td>
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    <td>14.326</td>
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</body>
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</html>
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===Modeling===
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X-ray and denovo modelling - AlphaFold2
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<p><img src="https://static.igem.wiki/teams/4165/wiki/model2.jpg" style="margin-left:200px;" alt="" width="500" /></p>
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</html>
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                  Figure 2.: A graphical illustration showing the structure of the inhibitor (X-Ray diffraction).
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/switches/12-alphafold.png" style="margin-left:200px;" alt="" width="500" /></p>
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</html>
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                  Figure 1.: A graphical illustration showing the structure of the inhibitor (AlphaFold).
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===References===
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1- HEINZEL, R., APPELHANS, H., GASSEN, G., SEEMÜLLER, U., MACHLEIDT, W., FRITZ, H., & STEFFENS, G. (1986). Molecular cloning and expression of cDNA for human antileukoprotease from cervix uterus. European journal of biochemistry, 160(1), 61-67.<br>
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2- Thompson, R. C., & Ohlsson, K. (1986). Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proceedings of the National Academy of Sciences, 83(18), 6692-6696.<br>
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3- Thompson, R. C., & Ohlsson, K. (1986). Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proceedings of the National Academy of Sciences, 83(18), 6692-6696.<br>
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4- Eisenberg, S. P., Hale, K. K., Heimdal, P., & Thompson, R. C. (1990). Location of the protease-inhibitory region of secretory leukocyte protease inhibitor. Journal of Biological Chemistry, 265(14), 7976-7981.<br>
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5- Mulligan, M. S., Lentsch, A. B., Huber-Lang, M., Guo, R. F., Sarma, V., Wright, C. D., ... & Ward, P. A. (2000). Anti-inflammatory effects of mutant forms of secretory leukocyte protease inhibitor. The American journal of pathology, 156(3), 1033-1039.<br>
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6- Fukushima, K., Kamimura, T., & Takimoto-Kamimura, M. (2013). Structure basis 1/2SLPI and porcine pancreas trypsin interaction. Journal of synchrotron radiation, 20(6), 943-947.<br>
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7- 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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8- 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>
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9- 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>
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<partinfo>BBa_K4165091 parameters</partinfo>
 
<partinfo>BBa_K4165091 parameters</partinfo>
 
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Latest revision as of 12:03, 13 October 2022


SLPI (Secretory leukocyte peptidase inhibitor).

This basic part encodes Human serine protease inhibitor secretory leukocyte peptidase inhibitor which is predicted to be able to inhibit HtrA1 (BBa_K4165004).

Usage and Biology

This type of inhibitor is considered to be an acid stable inhibitor with very high affinity for trypsins, chymotrypsine, elastases, and cathepsin G [1-6] . 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[7-9] .

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 219
  • 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)
67.2% 8.494 10.831 14.326


Modeling

X-ray and denovo modelling - AlphaFold2 


                 Figure 2.: A graphical illustration showing the structure of the inhibitor (X-Ray diffraction).




                 Figure 1.: A graphical illustration showing the structure of the inhibitor (AlphaFold).

References

1- HEINZEL, R., APPELHANS, H., GASSEN, G., SEEMÜLLER, U., MACHLEIDT, W., FRITZ, H., & STEFFENS, G. (1986). Molecular cloning and expression of cDNA for human antileukoprotease from cervix uterus. European journal of biochemistry, 160(1), 61-67.
2- Thompson, R. C., & Ohlsson, K. (1986). Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proceedings of the National Academy of Sciences, 83(18), 6692-6696.
3- Thompson, R. C., & Ohlsson, K. (1986). Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proceedings of the National Academy of Sciences, 83(18), 6692-6696.
4- Eisenberg, S. P., Hale, K. K., Heimdal, P., & Thompson, R. C. (1990). Location of the protease-inhibitory region of secretory leukocyte protease inhibitor. Journal of Biological Chemistry, 265(14), 7976-7981.
5- Mulligan, M. S., Lentsch, A. B., Huber-Lang, M., Guo, R. F., Sarma, V., Wright, C. D., ... & Ward, P. A. (2000). Anti-inflammatory effects of mutant forms of secretory leukocyte protease inhibitor. The American journal of pathology, 156(3), 1033-1039.
6- Fukushima, K., Kamimura, T., & Takimoto-Kamimura, M. (2013). Structure basis 1/2SLPI and porcine pancreas trypsin interaction. Journal of synchrotron radiation, 20(6), 943-947.
7- 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.
8- 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.
9- 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.