Difference between revisions of "Part:BBa K1075012"
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In had been shown that the LOV domain can be fused to entire protein domains, allowing photomodulation of the protein binding. However, Lungu et al. (2012) stated that it might be of high importance to bring the LOV domain closer to ipaA, in order to allow photomodulation in this case, because ipaA is only a peptide and thus more flexible than folded domains. | In had been shown that the LOV domain can be fused to entire protein domains, allowing photomodulation of the protein binding. However, Lungu et al. (2012) stated that it might be of high importance to bring the LOV domain closer to ipaA, in order to allow photomodulation in this case, because ipaA is only a peptide and thus more flexible than folded domains. | ||
| − | Therefore, Lungu et al. (2012) identified similar amino acid sequences in the ipaA peptide and the Ja helix of the LOV Domain and used this combined with molecular modeling to create photomodulateable AsLOV2-ipaA. | + | Therefore, Lungu et al. (2012) identified similar amino acid sequences in the ipaA peptide and the Ja helix of the LOV Domain and used this combined with molecular modeling to create photomodulateable AsLOV2-ipaA.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3334866/] |
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Latest revision as of 00:57, 5 October 2013
AsLOV2-ipaA
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.
In had been shown that the LOV domain can be fused to entire protein domains, allowing photomodulation of the protein binding. However, Lungu et al. (2012) stated that it might be of high importance to bring the LOV domain closer to ipaA, in order to allow photomodulation in this case, because ipaA is only a peptide and thus more flexible than folded domains.
Therefore, Lungu et al. (2012) identified similar amino acid sequences in the ipaA peptide and the Ja helix of the LOV Domain and used this combined with molecular modeling to create photomodulateable AsLOV2-ipaA.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3334866/]
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]