Coding

Part:BBa_K2719001:Design

Designed by: Karla Soto Blas   Group: iGEM18_TecCEM   (2018-08-08)


Tenascin Domain V

According to the information given from the phD Aurora Antonio, a beta-pleated sheet structure (antiparallel one) has a high level of stability but less than alpha-Helix. Also, it is possible to observe that this structure has many Random Coil, giving to the domain more flexibilite. In figure 1 you can see tenascin protein structure and it is conformed by beta-pleated antiparallel sheets and Random Coil, so that gives tenascin flexibility and stability.

"T--TecCEM--TCD5DomainV3DStructure.png"

Figure 2. Tenascin 5 domain V 3D structure, modelled with Swiss-Model


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
    COMPATIBLE WITH RFC[1000]



Design Notes

Optimized for E.coli BL21.


Source

Genomic Library

References

Laporte L., Jeffrey J., et. al.(2013).Tenascin C Promiscuously Binds Growth Factors via Its Fifth Fibronectin Type III-Like Domain. March 14, 2018, of NCBI Website: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3630135/

Gilpin, S. (2017) Fibrillin-2 and Tenascin-C bridge the age gap in lung epitelial regeneration. doi: 10.1016/j.biomaterials.2017.06.027.

Midwood, K. et al. (2003) Tissue repair and the dynamics of the extracelular matrix. doi:10.1016/j.biocel.2003.12.003

Midwood. K. et al. (2016) Tenascin-C at a glance. doi:10.1242/jcs.190546

Gnanou, Y., Leibler, L., and Matyjaszewski, K. (2007). Macromolecular Engineering. Precise Synthesis, Materials Properties, Applications. Weinheim, Germany: WILEY-VCH Verlag GmbH & Co. KGaA