Difference between revisions of "Part:BBa K4165076"
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | This type of family encodes for a type of inhibitor that is able to inhibit trypsins. The inhibitor is secreted from pancreatic acinar cells into the pancreatic juice. The main function of the inhibitor in pancreatic juice is the prevention of activation of immature trypsin zymogens within the pancreatic duct. 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 | + | This type of family encodes for a type of inhibitor that is able to inhibit trypsins. The inhibitor is secreted from pancreatic acinar cells into the pancreatic juice. The main function of the inhibitor in pancreatic juice is the prevention of activation of immature trypsin zymogens within the pancreatic duct. 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. |
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| − | <span class='h3bb'>Sequence and Features</span> | + | |
| + | ===<span class='h3bb'>Sequence and Features</span>=== | ||
<partinfo>BBa_K4165076 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4165076 SequenceAndFeatures</partinfo> | ||
| − | === | + | ===Dry Lab Characterization=== |
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| − | + | ===Modelling=== | |
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| − | + | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-inhibitors/spink1.png" style="margin-left:200px;" alt="" width="500" /></p> | |
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| − | + | Figure 1.: A graphical illustration showing the structure of SPINK1 (X-ray). | |
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| − | + | ===References=== | |
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| − | 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. | 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. | ||
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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. | 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. | ||
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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. | 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. | ||
<partinfo>BBa_K4165076 parameters</partinfo> | <partinfo>BBa_K4165076 parameters</partinfo> | ||
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Latest revision as of 23:50, 11 October 2022
SPINK1 (Serine Peptidase Inhibitor Kazal type 1).
This basic part encodes Human serine protease inhibitor known as SPINK1 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 inhibitor is secreted from pancreatic acinar cells into the pancreatic juice. The main function of the inhibitor in pancreatic juice is the prevention of activation of immature trypsin zymogens within the pancreatic duct. 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.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Dry Lab Characterization
Modelling
Figure 1.: A graphical illustration showing the structure of SPINK1 (X-ray).
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.