Part:BBa_K2719001:Design

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.

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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