Difference between revisions of "Part:BBa K4165085"
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===PDB Structure=== | ===PDB Structure=== | ||
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It has a predicted sturcture (AlphaFold2) | It has a predicted sturcture (AlphaFold2) | ||
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C-beta Deviations: | C-beta Deviations: | ||
Q-Mean: | Q-Mean: | ||
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| + | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/5-alphafold.png" style="margin-left:200px;" alt="" width="500" /></p> | ||
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| + | Figure 1.: A graphical illustration showing the structure of the inhibitor (AlphaFold). | ||
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===Reference===: | ===Reference===: | ||
Revision as of 14:18, 6 October 2022
SPINK14 (Serine Peptidase Inhibitor Kazal type 14).
This basic part encodes Human serine protease inhibitor known as SPINK14 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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Functional Parameters
GC% Content 62.2%
Isoelectric point (PI) 8.767
Charge at pH 7 5.898
Molecular Weight (Protein) 11.057 kDa
PDB Structure
It has a predicted sturcture (AlphaFold2)
AlphaFold:
https://alphafold.ebi.ac.uk/entry/Q6IE38
Molprobity:
Clash Score:
Ramachandran Favoured:
Ramachandran Outliers:
Rotamers Outliers:
C-beta Deviations:
Q-Mean:
Figure 1.: A graphical illustration showing the structure of the inhibitor (AlphaFold).
===Reference===: 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.