Difference between revisions of "Part:BBa K4020011"
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| − | + | ==Usage and Biology== | |
| + | SIDs (SRCR-interspersed domains) are roughly 20-amino-acid-long threonine-serine-proline-rich stretches consisting of a number of glycosylation sites that proposedly render the linkers to extended conformation, spanning 7 nm (Reichhardt et al., 2020; Turenchalk & Xu, 2001). They are intrinsically disordered regions separating the SRCR domains in the SALSA protein. It is synthetic DNA. | ||
| + | ==References== | ||
| + | *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 20:43, 18 October 2021
Usage and Biology
SIDs (SRCR-interspersed domains) are roughly 20-amino-acid-long threonine-serine-proline-rich stretches consisting of a number of glycosylation sites that proposedly render the linkers to extended conformation, spanning 7 nm (Reichhardt et al., 2020; Turenchalk & Xu, 2001). They are intrinsically disordered regions separating the SRCR domains in the SALSA protein. It is synthetic DNA.
References
- 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