Difference between revisions of "Part:BBa K2653000:Design"
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===Source=== | ===Source=== | ||
− | + | The sequence of trim21 comes from the article: James L C, Keeble A H, Khan Z, et al. Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function[J]. Proceedings of the National Academy of Sciences of the United States of America, 2007, 104(15):6200-6205. | |
===References=== | ===References=== | ||
+ | 1]Clift D, Mcewan W A, Labzin L I, et al. A Method for the Acute and Rapid Degradation of Endogenous Proteins[J]. Cell, 2017, 171(7):1692-1706.e18. | ||
+ | [2]Mcewan W A, Falcon B, Vaysburd M, et al. Cytosolic Fc receptor TRIM21 inhibits seeded tau aggregation.[J]. Proceedings of the National Academy of Sciences of the United States of America, 2017, 114(3):574. |
Latest revision as of 03:27, 18 October 2018
trim21
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 204
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 873
Illegal BamHI site found at 1411 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 161
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 1251
Design Notes
Trim21 has a special crab-shaped domain that can bind with the B30.2 domain of the Fc. Thus, with conservative Fc of the antibody binding with trim21, it then functions as a E3 ubiquitin ligase and proceeds the ubiquitin process of the antibody-antigen complex. Afterwards the proteasome depletes the target protein along with its antibody.
Source
The sequence of trim21 comes from the article: James L C, Keeble A H, Khan Z, et al. Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function[J]. Proceedings of the National Academy of Sciences of the United States of America, 2007, 104(15):6200-6205.
References
1]Clift D, Mcewan W A, Labzin L I, et al. A Method for the Acute and Rapid Degradation of Endogenous Proteins[J]. Cell, 2017, 171(7):1692-1706.e18. [2]Mcewan W A, Falcon B, Vaysburd M, et al. Cytosolic Fc receptor TRIM21 inhibits seeded tau aggregation.[J]. Proceedings of the National Academy of Sciences of the United States of America, 2017, 114(3):574.