Part:BBa_K4040000:Design
Intracellular Domain of the MEGF10 Protein
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 519
Design Notes
After the extracellular αS-scFv domain binds to the S protein of SARS-CoV-2, the intracellular cytosolic Immunoreceptor Tyrosine-based Activation Motifs (ITAMs) are activated with the help of the Src family kinases. And the SH2 binding domains for the protein expressing SH2 matching domains will be further exposed due to the space conformation change. The protein expressing SH2 matching domains, protein Syk, a phagocytic signaling effector can then active the downstream signaling transduction cascades and initiate the phagocytosis in our CARγ-macrophages eventually.
Source
The structure is also highly similar to the CARγ, with the only difference lying in the intracellular domain of the CAR, in which the common γ subunit of Fc receptors is replaced by MEGF10.