Difference between revisions of "Part:BBa K1075013"
| Line 4: | Line 4: | ||
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. | 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(<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. | + | 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.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3334866/] |
| − | |||
| − | |||
| − | |||
<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
Revision as of 00:59, 5 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.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3334866/]
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]