Difference between revisions of "Part:BBa K4020012"
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| − | + | ==Usage and Biology== | |
| + | SID linker (TEV site included) is a sequence of modified SID from SALSA protein with an integrated TEV protease recognition site. SIDs are roughly 20-amino-acid-long threonine-serine-proline-rich stretches of intrinsically disordered regions separating the SRCR domains in the SALSA protein. (Reichhardt et al., 2020; Turenchalk & Xu, 2001). TEV linker codes for the sequence of amino acids ENLYFQG/S, which TEV protease recognizes and cleaves between Q and G/S (Nam et al., 2020). It is synthetic DNA. | ||
| + | ==References== | ||
| + | *Nam, H., Hwang, B. J., Choi, D., Shin, S., & Choi, M. (2020). Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self‐cleavage exhibits enhanced enzymatic activity. FEBS Open Bio, 10(4), 619. https://doi.org/10.1002/2211-5463.12828 | ||
| + | *Reichhardt, M. P., Loimaranta, V., Lea, S. M., & Johnson, S. (2020). Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR fold. Life Science Alliance, 3(4). https://doi.org/10.26508/LSA.201900502 | ||
| + | *Turenchalk, G. S., & Xu, T. (2001). Lats in Cell-cycle Regulation and Tumorigenesis BT - Encyclopedic Reference of Cancer. Encyclopedic Reference of Cancer, 491–496. https://doi.org/10.1007/3-540-30683-8_944 | ||
Latest revision as of 20:48, 18 October 2021
Usage and Biology
SID linker (TEV site included) is a sequence of modified SID from SALSA protein with an integrated TEV protease recognition site. SIDs are roughly 20-amino-acid-long threonine-serine-proline-rich stretches of intrinsically disordered regions separating the SRCR domains in the SALSA protein. (Reichhardt et al., 2020; Turenchalk & Xu, 2001). TEV linker codes for the sequence of amino acids ENLYFQG/S, which TEV protease recognizes and cleaves between Q and G/S (Nam et al., 2020). It is synthetic DNA.
References
- Nam, H., Hwang, B. J., Choi, D., Shin, S., & Choi, M. (2020). Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self‐cleavage exhibits enhanced enzymatic activity. FEBS Open Bio, 10(4), 619. https://doi.org/10.1002/2211-5463.12828
- Reichhardt, M. P., Loimaranta, V., Lea, S. M., & Johnson, S. (2020). Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR fold. Life Science Alliance, 3(4). https://doi.org/10.26508/LSA.201900502
- Turenchalk, G. S., & Xu, T. (2001). Lats in Cell-cycle Regulation and Tumorigenesis BT - Encyclopedic Reference of Cancer. Encyclopedic Reference of Cancer, 491–496. https://doi.org/10.1007/3-540-30683-8_944