Difference between revisions of "Part:BBa K1742000:Design"

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===Design Notes===
 
===Design Notes===
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The LOv2 domain was fused to a small peptide epitope to the C-terminus of the J-alpha helix (-KAVDTWV). Depending on the nature of this peptide tag, its ligand ePDZ interacts with different interaction affinities.  
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The LOV2 domain was fused to a small peptide epitope to the C-terminus of the J-alpha helix (-KAVDTWV). Depending on the nature of this peptide tag, its ligand ePDZ interacts with different interaction affinities.  
 
The AsLOVpep domain also contains a linker 'GGSGGS-' in the N-terminus
 
The AsLOVpep domain also contains a linker 'GGSGGS-' in the N-terminus
  
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===References===
 
===References===
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Strickland D, Lin Y, Wagner E, Hope CM, Zayner J, Antoniou C, Sosnick TR, Weiss EL, Glotzer M (2012). TULIPs: tunable, light-controlled interacting protein tags for cell biology. Nat Methods 9:379-384

Latest revision as of 18:54, 14 September 2015


Avena sativa LOV2 domain


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

The LOV2 domain was fused to a small peptide epitope to the C-terminus of the J-alpha helix (-KAVDTWV). Depending on the nature of this peptide tag, its ligand ePDZ interacts with different interaction affinities. The AsLOVpep domain also contains a linker 'GGSGGS-' in the N-terminus

Source

The AsLOV2 fused to a peptide epitope was synthesized according to the second LOV domain of Avena sativa phototropin 1 (UniprotKB 049003)

References

Strickland D, Lin Y, Wagner E, Hope CM, Zayner J, Antoniou C, Sosnick TR, Weiss EL, Glotzer M (2012). TULIPs: tunable, light-controlled interacting protein tags for cell biology. Nat Methods 9:379-384