Difference between revisions of "Part:BBa K1075013"

 
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<partinfo>BBa_K1075013 short</partinfo>
 
<partinfo>BBa_K1075013 short</partinfo>
  
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Fusion of LOV 2 (A. sativa) with the ipaA peptide. It forms light inducable a tight dimer with Vinculin. [1]  
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Fusion of LOV 2 (''A. sativa'') with the ipaA peptide designed by Lungu et al. in 2012. It forms light inducable a tight dimer with Vinculin.
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Additional to their initial construct(<partinfo>BBa_K1075012</partinfo>) Lungu et al. further modified the system by mutations of the LOV-ipaA construct and successfully weakend the baseline affinity for vinculin (initial design: 3.5 nM to 69 nM; mutant: 2.4 nM to >40µM affinity for vinculin) to reduce the dark state activity.
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'''References'''
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[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3334866/]Lungu et al. (2012) Designing photoswitchable peptides using the AsLOV2 domain
  
 
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Revision as of 10:44, 4 October 2013

AsLOV2-ipaA(L623A)

Fusion of LOV 2 (A. sativa) with the ipaA peptide designed by Lungu et al. in 2012. It forms light inducable a tight dimer with Vinculin.

Additional to their initial construct(BBa_K1075012) Lungu et al. further modified the system by mutations of the LOV-ipaA construct and successfully weakend the baseline affinity for vinculin (initial design: 3.5 nM to 69 nM; mutant: 2.4 nM to >40µM affinity for vinculin) to reduce the dark state activity.

References

[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3334866/]Lungu et al. (2012) Designing photoswitchable peptides using the AsLOV2 domain

Sequence and Features


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]