Difference between revisions of "Part:BBa K2719006:Design"

Latest revision as of 03:27, 18 October 2018

Collagen V - Like

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
INCOMPATIBLE 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).

""

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

@@ Line 11: / Line 11: @@
 "https://static.igem.org/mediawiki/2018/0/0e/T--TecCEM--ColV2DStructure.png"
-<p>Figure 6. 2D structure of Collagen V-like</p>
+<p><i>Figure 6</i>. 2D structure of Collagen V-like</p>
 ===Source===
@@ Line 18: / Line 18: @@
 ===References===
+<p>Bächinger, H. P., Mizuno, K., Vranka, J. A., & Boudko, S. P. (2010). <i>Collagen formation and structure. In Comprehensive Natural Products II: Chemistry and Biology </i>(Vol. 5, pp. 469-530). Elsevier Ltd.</p>
+<p>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. <i>The Journal of Biological Chemistry</i>, 278(1), 645-650.</p>
+<p>Hashimoto, K., Ito, M., Kato, I., Koitabashi, H., Takahara, K., and Yaoi, Y. (1990). Primary structure of heparin-binding site of type V collagen. <i>Biochimica et Biophysica Acta</i>, 1035, 139-145.</p>
+<p>Liu, S. (2007). Bioregenerative Engineering: Principles and Applications. <i>Wiley-Interscience</i>. pp. 102-108</p>
+<p>Rutschmann, C., Baumann, S., Cabalzar, J., Luther, K. B., & Hennet, T. (2014). Recombinant expression of hydroxylated human collagen in escherichia coli. <i>Applied Microbiology and Biotechnology</i>, 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</p>
+<p>An B., Kaplan D. & Brodsky B. (2014). Engineered recombinant bacterial collagen as an alternative collagen-based biomaterial for tissue engineering. <i>Frontiers in Chemistry</i>. Doi: 10.3389/fchem.2014.00040</p>