Difference between revisions of "Part:BBa K4165088"
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X-ray
 
X-ray
 
https://www.rcsb.org/structure/1FLE
 
https://www.rcsb.org/structure/1FLE
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Q_Mean =
 
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Ramachandran Favoured =
 
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<html>
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<p><img src="https://static.igem.wiki/teams/4165/wiki/model3.jpg" style="margin-left:200px;" alt="" width="500" /></p>
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                  Figure 1.: A graphical illustration showing the domains of TRIM21 (X-Ray diffraction).
  
  
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NMR:
 
NMR:
 
https://www.rcsb.org/structure/2REL
 
https://www.rcsb.org/structure/2REL
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Q_Mean =
 
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Clash Score =
 
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Total Score =
 
  
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<p><img src="https://static.igem.wiki/teams/4165/wiki/model4.jpg" style="margin-left:200px;" alt="" width="500" /></p>
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</html>
  
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                  Figure 2.: A graphical illustration showing the domains of TRIM21 (NMR).
  
 
AlphaFold
 
AlphaFold
 
https://alphafold.ebi.ac.uk/entry/P19957
 
https://alphafold.ebi.ac.uk/entry/P19957
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</html>
  
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                   Figure 1.: A graphical illustration showing the domains of TRIM21.
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                   Figure 3.: A graphical illustration showing the domains of TRIM21 (AlphaFold).
  
 
===References===
 
===References===

Revision as of 00:18, 12 October 2022


WAP-four disulfide core domain 14 serine protease inhibitor.

This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 14 which is able to inhibit HtrA1 (BBa_K4165004).


Usage and Biology

This type of family encodes for a type of inhibitor that contains a motif which consists of 8 cysteine residues capable of forming four disulfide bonds at the core of the protease, thus inhibiting its action. The main function of this inhibitor is to prevent elastase-mediated tissue proteolysis. This type of inhibitor is very effective and has high affinity for trypsin-like proteases (serine proteases), and in our case it would act as an inhibitor for the trypsin-like catalytic domain of serine protease HtrA1[1-3].


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 132
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 189
  • 1000
    COMPATIBLE WITH RFC[1000]


Functional Parameters

GC Content% 67.5%

Isoelectric point (PI) 8.641

Charge at pH 7 6.373

Molecular Weight (Protein) 12.27 kDa

PDB structure

X-ray, NMR, and the predicted structures (AlphaFold2) are all present.

X-ray https://www.rcsb.org/structure/1FLE 

                 Figure 1.: A graphical illustration showing the domains of TRIM21 (X-Ray diffraction).


NMR: https://www.rcsb.org/structure/2REL 

                 Figure 2.: A graphical illustration showing the domains of TRIM21 (NMR).

AlphaFold https://alphafold.ebi.ac.uk/entry/P19957 


                 Figure 3.: A graphical illustration showing the domains of TRIM21 (AlphaFold).

References

1. Clauss, A., Lilja, H., & Lundwall, Å. (2005). The evolution of a genetic locus encoding small serine proteinase inhibitors. Biochemical and biophysical research communications, 333(2), 383-389.
2. 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. 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.