| Types | DnaRegion
|
| Roles | Coding
CDS
|
| Sequences | BBa_K1742000_sequence (Version 1)
|
Description
Plants and bacteria contain a variety of photoreceptors that activate intracellular signalling in response ti light. Among these, the most extensively studied are LOV (light/oxygen/voltage) domains. On blue light (peak 450nm) aabsorption, the FMN cofactor in the LOV domain forms a covalent bond with a cysteine residue. In the LOV2 domain of plant phototropin, the FMN-cysteine bond formation leads to partial unfolding of the C-terminal alpha-helix from the rest of the LOV2 domain. Strickland et al. created LOV2 fusions capable of light-mediated heterodimerization by fusing the LOV2 domain to peptides that bind to PDZ domains.
Notes
The LOv2 domain was fused to a small peptide epitope to the C-terminus of the J-alpha helix (-KAVDTWV). Depending on this peptide, the engineered variants of the Erbin PDZ domains would vary in interaction affinity.
Source
The AsLOV2 fused to a peptide epitope was designed according to the second LOV domain of Avena sativa phototropin (UniprotKB 049003)
