Difference between revisions of "Part:BBa K4165076"
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===Usage and Biology===
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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 [1] - [3].
 
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 [1] - [3].
  
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===Parameters===
 
GC% Content
 
GC% Content
 
56.5%
 
56.5%

Revision as of 16:48, 5 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 [1] - [3].


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Parameters

GC% Content 56.5%

Isoelectric point (PI) 7.338

Charge at pH 7 0.508

Molecular Weight (Protein) 8.507 kDa

It has both x-ray structure and a predicted model (AlphaFold2). PDB structure

X-ray structure: https://drive.google.com/drive/folders/1o_e_vCFs-bwbqS0z-3XsDzY9ENKnag4I 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

AlphaFold: 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

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.