Part:BBa_K1462503:Design
SH3 domain + Linker
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 196
Illegal XhoI site found at 177 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
The SH3 domain + linker is the fusion unit of the scaffold protein and help the targeted emzyme to bind on. So we added the linker behind it and help do the next job.
Source
We got it from the synthesis of Genewiz.
References
[1] John E Dueber, Gabriel C Wu, G Reza Malmirchegini, et al.Synthetic protein scaffolds provide modular control over metabolic flux.Nat Biotechnol. 2009 Aug;27(8):753-9. [2] Schultz, J. et al. Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels. Nat Struct Biol 5, 19-24 (1998). [3] Kim, A.S., Kakalis, L.T., Abdul-Manan, N., Liu, G.A. & Rosen, M.K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404, 151-158 (2000). [4] Wu, X. et al. Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure 3, 215-226 (1995). [5] Harris, B.Z., Hillier, B.J. & Lim, W.A. Energetic determinants of internal motif recognition by PDZ domains. Biochemistry 40, 5921-5930 (2001). [6] Dueber, J.E., Yeh, B.J., Chak, K. & Lim, W.A. Reprogramming control of an allosteric signaling switch through modular recombination. Science 301, 1904-1908 (2003). [7] Nguyen, J.T., Turck, C.W., Cohen, F.E., Zuckermann, R.N. & Lim, W.A. Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors. Science 282, 2088-2092 (1998).