Major histocompatibility complex-peptide complex on dendritic cell and T-cell receptor on T lymphocyte (MHC-peptide complex and TCR)

The major histocompatibility complex (MHC)-peptide complex is formed by MHC class I or class II proteins on the surface of antigen-presenting cells such as dendritic cells, which bind short peptides derived from foreign or self proteins. This complex is essential for the presentation of antigens to T cells. The T-cell receptor (TCR) is found on T lymphocytes and recognizes specific peptides presented by MHC molecules, triggering T-cell activation and orchestrating adaptive immune responses. The interaction between the MHC-peptide complex and the TCR is a central event in immune surveillance, vaccine response, cancer immunotherapy, and autoimmunity, with therapeutic targeting mostly focused on engineered TCRs, peptide vaccines, or biologics that manipulate TCR-pMHC recognition[1][3][5][6]. Structural studies have elucidated the canonical interaction mode and key features that govern antigen specificity, but high diversity and complex regulation present ongoing challenges for therapy design[2][6].

Other names

MHC class I/II-peptidepMHCpeptide-MHC complexantigen-presenting complexTCRT-cell antigen receptor

Direct TCR binding to peptide-MHC complex leads to T-cell activation and subsequent killing, cytokine production, or immune modulation. TCR engineered drugs may redirect T cells to tumors, increasing immune attack.