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 Human serine protease inhibitor known as SPINK8 which is able to inhibit trypsin-like proteases, like 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 serine proteaseHtrA1 (BBa_K4165004).
  
 
===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 <sup>[1-3]</sup>.
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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.
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===<span class='h3bb'>Sequence and Features</span>===
 
===<span class='h3bb'>Sequence and Features</span>===
 
<partinfo>BBa_K4165010 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4165010 SequenceAndFeatures</partinfo>
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===Dry Lab Characterization===
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<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
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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.
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===Functional Parameters===
 
===Functional Parameters===
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10.821 kDa
 
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:
 
  
 
===References===
 
===References===

Revision as of 17:04, 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 proteaseHtrA1 (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


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]


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.


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.