Difference between revisions of "Part:BBa K4165089"
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===Functional Parameters=== | ===Functional Parameters=== | ||
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+ | <th>GC Content%</th> | ||
+ | <th>Isoelectric point (PI)</th> | ||
+ | <th>Charge at pH 7</th> | ||
+ | <th>Molecular Weight (Protein)</th> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td>68.8%</td> | ||
+ | <td>4.371</td> | ||
+ | <td>-4.23</td> | ||
+ | <td>12.993 kDa</td> | ||
+ | </tr> | ||
+ | </table> | ||
+ | </body> | ||
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===PDB structure=== | ===PDB structure=== | ||
The predicted structure (AlphaFold2) is presented. | The predicted structure (AlphaFold2) is presented. | ||
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Latest revision as of 12:10, 13 October 2022
WAP-four disulfide core domain 2 serine protease inhibitor.
This basic part encodes Human serine protease inhibitor WAP-four disulfide core domain 2 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 pervent 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
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 115
Illegal PstI site found at 183 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 115
Illegal PstI site found at 183 - 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 115
Illegal PstI site found at 183 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 115
Illegal PstI site found at 183
Illegal NgoMIV site found at 3 - 1000COMPATIBLE WITH RFC[1000]
Functional Parameters
GC Content% | Isoelectric point (PI) | Charge at pH 7 | Molecular Weight (Protein) |
---|---|---|---|
68.8% | 4.371 | -4.23 | 12.993 kDa |
PDB structure
The predicted structure (AlphaFold2) is presented.
Figure 1.: A graphical illustration showing the structure of the inhibitor.
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.