Difference between revisions of "Part:BBa K4165010"

 
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<partinfo>BBa_K4165010 short</partinfo>
 
<partinfo>BBa_K4165010 short</partinfo>
  
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This basic part encodes for Human serine protease inhibitor Kazal type 8 (SPINK8) which is able to inhibit HtrA1 (BBa_K4165004)  
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This basic part encodes Human serine protease inhibitor known as SPINK8 which is able to inhibit trypsin-like proteases, like HtrA1 (BBa_K4165004).
  
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<!-- Add more about the biology of this part here
 
 
===Usage and Biology===
 
===Usage and Biology===
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This type of family encodes for a type of inhibitor that is predicted to be able to inhibit serine peptidases. The inhibitor is present extracellularly. The inhibitor 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 [1] - [3].
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===Functional Parameters===
 
===Functional Parameters===
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GC% Content
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61.2%
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Isoelectric point (PI)
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4.597
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Charge at pH 7
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-3.459
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Molecular Weight (Protein)
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10.821 kDa
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===PDB Structure===
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It is a predicted model (AlphaFold2).
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AlphaFold:
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https://alphafold.ebi.ac.uk/entry/P0C7L1
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Molprobity:
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Clash Score:
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Ramachandran Favoured:
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Ramachandran Outliers:
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Rotamers Outliers:
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C-beta Deviations:
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Q-Mean:
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===References===
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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.
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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.
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<partinfo>BBa_K4165010 parameters</partinfo>
 
<partinfo>BBa_K4165010 parameters</partinfo>
 
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Revision as of 19:37, 5 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 HtrA1 (BBa_K4165004).

Usage and Biology

This type of family encodes for a type of inhibitor that is predicted to be able to inhibit serine peptidases. The inhibitor is present extracellularly. The inhibitor 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 [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]


Functional Parameters

GC% Content 61.2%

Isoelectric point (PI) 4.597

Charge at pH 7 -3.459

Molecular Weight (Protein) 10.821 kDa

PDB Structure

It is a predicted model (AlphaFold2).

AlphaFold: https://alphafold.ebi.ac.uk/entry/P0C7L1 Molprobity: Clash Score: Ramachandran Favoured: Ramachandran Outliers: Rotamers Outliers: C-beta Deviations: Q-Mean:

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.