Part:BBa_K4803000
gp130 (IL 6 receptor-beta) extracellular domain
Usage and Biology
Glycoprotein130 (gp130) is, known as interleukin 6 signal transducer(IL6ST) or Interleukin 6 Receptor-β (IL6R-β), one of the cytokine receptor which functions in mammalian cell. This protein is ubiquitously expressed in the human body and forms a gp130-IL6-gp80 trimer in the presence of IL6. The trimer also binds to each other to form a hexamer. This hexamer formation reaction mediates cytokine signaling by activating the associated cytosolic tyrosine kinase and subsequent modification of transcription factors [1][2][3].
The sequence of this part is an extracellular domain generated by codon optimization of the gp130 cDNA described in [1], minus the 5' end signal and downstream of the transmembrane region. In UTokyo2023 project, this part was used as part of the MESA (Modular Extracellular Sensor Architecture) system. This part forms homodimers or heterodimers with gp80 (BBa_K4803001) in the presence of IL6, which allows intracellular proteases to act and release protein of interest into the cytosol.
Characterization
In UTokyo2023 project, the 3D structure of this part was predicted by LocalColabFold [4].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 9
Illegal BamHI site found at 827 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
[1] Hibi, M., Murakami, M., Saito, M., Hirano, T., Taga, T., & Kishimoto, T. (1990). Molecular cloning and expression of an IL-6 signal transducer, gp130. Cell, 63(6), 1149-1157. https://doi.org/10.1016/0092-8674(90)90411-7
[2] Taga, T., & Kishimoto, T. (1997). Gp130 and the interleukin-6 family of cytokines. Annual review of immunology, 15(1), 797-819. https://doi.org/10.1146/annurev.immunol.15.1.797
[3] Kaur, S., Bansal, Y., Kumar, R., & Bansal, G. (2020). A panoramic review of IL-6: Structure, pathophysiological roles and inhibitors. Bioorganic & medicinal chemistry, 28(5), 115327. https://doi.org/10.1016/j.bmc.2020.115327
[4] Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2022). ColabFold: Making protein folding accessible to all. Nature Methods, 19(6), 679-682. https://doi.org/10.1038/s41592-022-01488-1
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