Difference between revisions of "Part:BBa K1497025"
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The SH3 domain and its ligand (<a href="/Part:BBa_KK771108">BBa_KK771108</a>) are suitable tools for protein colocalizaion. Initially, the domain was a part of the Crk protein in Mus musculus. The SH3 domain is used as a binding unit of the so-called protein scaffold published by Dueber et al. in 2012. The scaffold (<a href="/Part:BBa_KK1497033">BBa_KK1497033</a>) is composed of different binding units, which enable the assembly of multiple target proteins. This BioBrick adds a BglII and BamHI restriction site in front of and behind the previously constructed domain sequence (<a href="/Part:BBa_KK771107">BBa_KK771107</a>). Now, different binding units of the scaffold protein can be fused together without the introduction of restriction sites.  This allows the easy construction of BioBricks of different permutations of the scaffold protein domains.
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The SH3 domain and its ligand (<a href="/Part:BBa_K771108">BBa_K771108</a>) are suitable tools for protein colocalizaion. Initially, the domain was a part of the Crk protein in Mus musculus. The SH3 domain is used as a binding unit of the so-called protein scaffold published by Dueber et al. in 2012. The scaffold (<a href="/Part:BBa_K1497033">BBa_K1497033</a>) is composed of different binding units, which enable the assembly of multiple target proteins. This BioBrick adds a BglII and BamHI restriction site in front of and behind the previously constructed domain sequence (<a href="/Part:BBa_K771107">BBa_K771107</a>). Now, different binding units of the scaffold protein can be fused together without the introduction of restriction sites.  This allows the easy construction of BioBricks of different permutations of the scaffold protein domains.
 
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Revision as of 13:57, 11 October 2014

SH3-Domain


The SH3 domain and its ligand (BBa_K771108) are suitable tools for protein colocalizaion. Initially, the domain was a part of the Crk protein in Mus musculus. The SH3 domain is used as a binding unit of the so-called protein scaffold published by Dueber et al. in 2012. The scaffold (BBa_K1497033) is composed of different binding units, which enable the assembly of multiple target proteins. This BioBrick adds a BglII and BamHI restriction site in front of and behind the previously constructed domain sequence (BBa_K771107). Now, different binding units of the scaffold protein can be fused together without the introduction of restriction sites. This allows the easy construction of BioBricks of different permutations of the scaffold protein domains.

Figure 1 .

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 1
    Illegal BamHI site found at 226
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


References

Dueber, John E.; Wu, Gabriel C.; Malmirchegini, G. Reza; Moon, Tae Seok; Petzold, Christopher J.; Ullal, Adeeti V. et al. (2009): Synthetic protein scaffolds provide modular control over metabolic flux. In Nat. Biotechnol. 27 (8), pp. 753–759. DOI: 10.1038/nbt.1557.
Wu, X.; Knudsen, B.; Feller, S. M.; Zheng, J.; Sali, A.; Cowburn, D. et al. (1995): Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. In Structure 3 (2), pp. 215–226.