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The Human papillomavirus type 16 E7 oncoprotein peptide–HLA-A*02:01 complex refers to a specific peptide derived from the HPV-16 E7 oncoprotein presented by the human major histocompatibility complex (MHC) class I allele HLA-A*02:01 on the surface of infected or transformed cells. HPV-16 E7 is a 98-residue multifunctional nuclear phosphoprotein and viral oncoprotein that drives cell cycle progression from G1 to S phase, enabling viral genome replication, and inactivates tumor suppressors like pRB to promote oncogenesis in high-risk HPV infections, particularly cervical cancer[1][2][5][8]. The E7 protein features a disordered N-terminal domain (E7N, residues 1-40 with conserved regions CR1 and CR2) that is flexible and promiscuous for binding cellular partners, and a structured C-terminal domain (E7C, residues 41-98 with CR3) that forms a zinc-binding globular fold with β-sheet and α-helical elements, existing predominantly as a dimer in equilibrium with a minor monomeric state[1]. In immunotherapy contexts, peptides from E7 (e.g., immunogenic epitopes like those in CR2/3 regions) are loaded onto HLA-A*02:01 to form peptide-MHC complexes recognized by cytotoxic CD8+ T cells, serving as targets for cancer vaccines and T-cell therapies against HPV-associated malignancies[4][8]. This complex highlights E7's role as a tumor-specific antigen due to its expression in transformed cells but not healthy tissues[5][8].
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