Difference between revisions of "Part:BBa K4165079"
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<partinfo>BBa_K4165079 short</partinfo> | <partinfo>BBa_K4165079 short</partinfo> | ||
− | + | This basic part encodes Human serine protease inhibitor known as SPINK2 which is able to inhibit trypsin-like proteases, like HtrA1 (BBa_K4165004). | |
− | |||
===Usage and Biology=== | ===Usage and Biology=== | ||
+ | This type of family encodes for a type of inhibitor that is able to inhibit trypsins. The main function of the inhibitor is hindering the premature activation of proacrosin and many other proteases, thus preventing defects in the spermiogenesis process. The inhibitor binds to trypsin proteases and since the catalytic core of HtrA1 (BBa_K4165004) is considered as a trypsin-like catalytic domain, so this inhibitor also is considered to inhibit the function of HtrA1 [1] - [3]. | ||
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− | <span class='h3bb'>Sequence and Features</span> | + | ===<span class='h3bb'>Sequence and Features</span>=== |
<partinfo>BBa_K4165079 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4165079 SequenceAndFeatures</partinfo> | ||
− | < | + | ===Dry-Lab Characterization=== |
− | === | + | |
+ | ===Modelling=== | ||
+ | |||
+ | |||
+ | <html> | ||
+ | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/switches/p20155-xray.png" style="margin-left:200px;" alt="" width="500" /></p> | ||
+ | </html> | ||
+ | |||
+ | Figure 1.: A graphical illustration showing the structure of the inhibitor (X-ray). | ||
+ | |||
+ | |||
+ | |||
+ | |||
+ | <html> | ||
+ | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/switches/p20155-nmr.png" style="margin-left:200px;" alt="" width="500" /></p> | ||
+ | </html> | ||
+ | |||
+ | Figure 2.: A graphical illustration showing the structure of the inhibitor (NMR). | ||
+ | |||
+ | ===References=== | ||
+ | 1 - Frochaux, V., Hildebrand, D., Talke, A., Linscheid, M. W., & Schlüter, H. (2014). Alpha-1-antitrypsin: a novel human high temperature requirement protease A1 (HTRA1) substrate in human placental tissue. PloS one, 9(10), e109483. <br> | ||
+ | 2 - 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> | ||
+ | 3 - 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> | ||
+ | |||
<partinfo>BBa_K4165079 parameters</partinfo> | <partinfo>BBa_K4165079 parameters</partinfo> | ||
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Latest revision as of 00:37, 12 October 2022
SPINK2 (Serine Peptidase Inhibitor Kazal type 2).
This basic part encodes Human serine protease inhibitor known as SPINK2 which is able to inhibit trypsin-like proteases, like HtrA1 (BBa_K4165004).
Usage and Biology
This type of family encodes for a type of inhibitor that is able to inhibit trypsins. The main function of the inhibitor is hindering the premature activation of proacrosin and many other proteases, thus preventing defects in the spermiogenesis process. The inhibitor binds to trypsin proteases and since the catalytic core of HtrA1 (BBa_K4165004) is considered as a trypsin-like catalytic domain, so this inhibitor also is considered to inhibit the function of HtrA1 [1] - [3].
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 105
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 105
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 105
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 105
- 1000COMPATIBLE WITH RFC[1000]
Dry-Lab Characterization
Modelling
Figure 1.: A graphical illustration showing the structure of the inhibitor (X-ray).
Figure 2.: A graphical illustration showing the structure of the inhibitor (NMR).
References
1 - Frochaux, V., Hildebrand, D., Talke, A., Linscheid, M. W., & Schlüter, H. (2014). Alpha-1-antitrypsin: a novel human high temperature requirement protease A1 (HTRA1) substrate in human placental tissue. PloS one, 9(10), e109483.
2 - 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 - 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.