Difference between revisions of "Part:BBa K4165010"
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This inhibitor was modeled using different software (trRosetta - AlphaFold2 - RosettaFold - Modeller) and the top model was acquired from trRosetta ranking 6 out of 6 according to our Quality Assesment code. | This inhibitor was modeled using different software (trRosetta - AlphaFold2 - RosettaFold - Modeller) and the top model was acquired from trRosetta ranking 6 out of 6 according to our Quality Assesment code. | ||
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+ | Figure 1. Predicted 3D structure of SPINK8 inhibitor | ||
===Functional Parameters=== | ===Functional Parameters=== |
Revision as of 17:33, 10 October 2022
Human serine protease inhibitor Kazal type 8 (SPINK8)
This basic part encodes Human serine protease inhibitor known as SPINK8 which is able to inhibit trypsin-like proteases like serine protease HtrA1 (BBa_K4165004).
Usage and Biology
This type of family encodes inhibitors that is predicted to be able to inhibit serine peptidases. The inhibitor is present extracellularly and binds to trypsin-like proteases (serine 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
Modeling
This inhibitor was modeled using different software (trRosetta - AlphaFold2 - RosettaFold - Modeller) and the top model was acquired from trRosetta ranking 6 out of 6 according to our Quality Assesment code.
Figure 1. Predicted 3D structure of SPINK8 inhibitor
Functional Parameters
GC% Content 61.2%
Isoelectric point (PI) 4.597
Charge at pH 7 -3.459
Molecular Weight (Protein) 10.821 kDa
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.