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The **T-cell receptor–major histocompatibility complex immunological synapse** is not a single molecule or typical drug target but rather a specialized structure formed at the interface between a T cell and an antigen-presenting cell (APC). During this process, the **T-cell receptor (TCR)** on the T cell surface recognizes and binds to antigenic peptides presented by the **major histocompatibility complex (MHC)** molecules on the APC. Engagement of TCR and peptide–MHC (pMHC) initiates intracellular signaling, cytoskeletal rearrangement, and results in focused secretion of cytokines and other effector responses[1][2][4]. This **immunological synapse** ensures high specificity in antigen recognition, leading to T-cell activation, proliferation, cytotoxicity, and immune modulation[1][9]. Its formation is essential for robust signal transduction and the development of immune responses, but is itself a supramolecular structure—not directly a molecule, enzyme, or receptor that can be targeted pharmacologically. Therefore, it should not be listed as a canonical therapeutic target as defined by individual proteins (such as receptors or enzymes), and groups too much information under a single label[1][2][4][9]. *Note:* For detailed data on druggability, mechanisms, or biomarkers, refer specifically to the molecular components—T-cell receptor and major histocompatibility complex class I or II molecules—rather than the synapse as a whole.
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