[5] Additionally this domain can be incorporated into chimeric antigen receptor (CAR) designs for T cell therapies that allows for the specific recognition and binding of target antigens, such as CD123, which is a potential therapeutic target for hematologic malignancies like acute myelogenous leukemia (AML).
Interactions with the adjacent thyroid hormone receptor ligand-binding domain's (TR-LBD), AF-2 coactivator-binding groove are necessary for the creation of the H0 structure of D-domain.
[4][5] The unique topology of D-domain enables it to target epitopes that may not be accessible to scFv CDR loops, offering the potential for improved antigen recognition.
[7] In addition, it can be engineered to be less immunogenic by removing putative T cell epitopes, potentially reducing the risk of antigen-independent exhaustion.
[6] On the other hand, trivial effect on phosphorylation is observed due to mutation at the D-domain of p38MAPKs, which signifies the inertness of this domain to the interaction of Elk-1 to p38 MAPKs.
[4] Also, dimerization of the SCF complex facilitated by the D-domain shows insignificant overtly impact on catalytic competence or substrate affinity but enhances lysine acceptor site utilization.