Part:BBa_K2719006:Design
Collagen V - Like
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 92
Design Notes
As in humans collagen requires the hydroxylation of proline for the proper formation of the tertiary structure and its correct function. Since it is difficult to induce postraductional modifications in a prokaryotic system, this part was designed for the incorporation of hydroxyproline as a non-canonical amino acid. Thus eliminating the need of post traductional modifications. In order to allow the incorporation of non-canonical amino acids, this sequence was optimized for E.coli Rosetta (DE3).
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Figure 6. 2D structure of Collagen V-like
Source
Genomic sequence
References
Bächinger, H. P., Mizuno, K., Vranka, J. A., & Boudko, S. P. (2010). Collagen formation and structure. In Comprehensive Natural Products II: Chemistry and Biology (Vol. 5, pp. 469-530). Elsevier Ltd.
Brown, M., Buechter, D., Gruskin, E., Leslie, B., Mehos, K., and Paolella, D. (2003). Co-translational Incorporation of Trans-4-Hydroxyproline into Recombinant Proteins in Bacteria. The Journal of Biological Chemistry, 278(1), 645-650.
Hashimoto, K., Ito, M., Kato, I., Koitabashi, H., Takahara, K., and Yaoi, Y. (1990). Primary structure of heparin-binding site of type V collagen. Biochimica et Biophysica Acta, 1035, 139-145.
Liu, S. (2007). Bioregenerative Engineering: Principles and Applications. Wiley-Interscience. pp. 102-108
Rutschmann, C., Baumann, S., Cabalzar, J., Luther, K. B., & Hennet, T. (2014). Recombinant expression of hydroxylated human collagen in escherichia coli. Applied Microbiology and Biotechnology, 98(10), 4445-55. http://0-dx.doi.org.millenium.itesm.mx/10.1007/s00253-013-5447-z Retrieved from http://0-search.proquest.com.millenium.itesm.mx/docview/1519819493?accountid=11643
An B., Kaplan D. & Brodsky B. (2014). Engineered recombinant bacterial collagen as an alternative collagen-based biomaterial for tissue engineering. Frontiers in Chemistry. Doi: 10.3389/fchem.2014.00040