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The KRAS mutant peptide-HLA-A*11:01 complex is formed when peptides derived from mutant forms of KRAS, particularly those carrying oncogenic mutations such as G12V or G12D, are presented on the cell surface by the MHC class I molecule HLA-A*11:01. This complex is specifically recognized by T-cell receptors, enabling the immune system to target and destroy cancer cells bearing the KRAS mutation. Structural studies have shown that different KRAS mutant peptides engage HLA-A*11:01 with varying affinities and conformations, which directly influence TCR recognition and therapeutic potential. Recent research has demonstrated that TCR-based therapies targeting this complex can have robust anti-tumor activity, but safety considerations such as cross-reactivity with self-peptides must be carefully managed. The presence of the HLA-A*11:01 allele and KRAS mutations serves as key biomarkers for patient selection in these immunotherapeutic approaches[1][3][5][7].
Recognition and killing of tumor cells by T cells via engineered T-cell receptors that specifically bind to the KRAS mutant peptide-HLA-A*11:01 complex Immune system activation against cells presenting mutant KRAS peptides
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