Difference between revisions of "Part:BBa K4165078"
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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 serine peptidases, especially kallkreins. The inhibitor’s main function is to inhibit kallikrein-related peptidases in the skin. The inhibitor binds to serine peptidases and since the catalytic core of HtrA1 (BBa_K4165004) is considered as a serine catalytic domain, so this inhibitor also is considered to inhibit the function of HtrA1 [1 | + | This type of family encodes for a type of inhibitor that is able to inhibit serine peptidases, especially kallkreins. The inhibitor’s main function is to inhibit kallikrein-related peptidases in the skin. The inhibitor binds to serine peptidases and since the catalytic core of HtrA1 (BBa_K4165004) is considered as a serine catalytic domain, so this inhibitor also is considered to inhibit the function of HtrA1 <sup>[1-3]</sup>. |
| Line 70: | Line 70: | ||
===References=== | ===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. <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. | + | 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. | 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. | ||
Revision as of 18:22, 10 October 2022
SPINK6 (Serine Peptidase Inhibitor Kazal type 6).
This basic part encodes Human serine protease inhibitor known as SPINK6 which is able to inhibit serine peptidases.
Usage and Biology
This type of family encodes for a type of inhibitor that is able to inhibit serine peptidases, especially kallkreins. The inhibitor’s main function is to inhibit kallikrein-related peptidases in the skin. The inhibitor binds to serine peptidases and since the catalytic core of HtrA1 (BBa_K4165004) is considered as a serine catalytic domain, so this inhibitor also is considered to inhibit the function of HtrA1 [1-3].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 102
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Functional Parameters
GC% Content 54.6% Isoelectric point (PI) 8.117 Charge at pH 7 3.635 Molecular Weight (Protein) 8.585 kDa
It has both NMR structure and a predicted model (AlphaFold2).
PDB structure: https://drive.google.com/drive/folders/1OhqZoqIootmRPpiVkemM_npNaA5WMO9b
NMR structure: https://www.rcsb.org/structure/2N52 Molprobity: 2.47 Clash Score: 9.35 Ramachandran Favoured: 94.44% Ramachandran Outliers: 0% Rotamers Outliers: 6% C-beta Deviations: 0% Q-Mean: 0.83 土 0.11
Figure 1.: A graphical illustration showing the structure of the inhibitor (NMR).
AlphaFold2: https://drive.google.com/drive/folders/1o_e_vCFs-bwbqS0z-3XsDzY9ENKnag4I Molprobity: 1.11 Clash Score: 0 Ramachandran Favoured: 92.21% Ramachandran Outliers: 0% Rotamers Outliers: 1.49% C-beta Deviations: 0% Q-Mean: 0.65 土 0.1
Figure 2.: A graphical illustration showing the structure of the inhibitor (AlphaFold).
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.