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The **major histocompatibility complex–T cell receptor interface** is a critical site where antigen-presenting cells display peptide antigens bound to MHC molecules, allowing recognition by T cell receptors on lymphocytes. This interface initiates downstream signaling events culminating in T cell activation, cytokine release, and immune effector functions[2][4][1]. The structural interaction involves the variable domains of both MHC molecules and TCRs, with stabilization by accessory molecules such as CD3, CD4/CD8, and signal transducing kinases (e.g., Lck)[2][6]. Therapeutic targeting of this interface can modulate immune responses in cancer, infection, autoimmunity, and transplant rejection. Notably, bacterial superantigens can exploit this interface to induce massive T cell activation and cytokine storms[3][5]. This "target" describes a molecular event/interface, not a discrete molecule, and requires clarification for structured data entry.
Inhibition or activation of T cell signaling through modulation of MHC–TCR interactions; Induction of T cell anergy or cytotoxicity; Blocking antigen presentation; Enhancement or suppression of immune synapse formation
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