9x7u | pdb_00009x7u
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Complex of HLA-A2, a class I MHC, with a UTP20 peptide
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Structural highlights
FunctionPublication Abstract from PubMedAdoptive T cell therapy (ACT) eliminates tumors by infusing tumor reactive T cells. Neoantigens from somatic mutations are ideal targets due to their absence in normal tissues. How charge-reversing mutations drive neoantigen immunogenicity remains unclear. Here, we determined the wild-type and mutant UTP20-HLA-A2 structures and found them nearly identical except at the mutation site (Asp to His). The TCR-pHLA structure revealed selective recognition through specific interactions between CDR loops and the mutation site. Rosetta calculations showed that His provides favorable interactions absent in the wild-type. TCR engagement also induced a flip of the P6 side chain, reshaping the interface. These findings provide a structural basis for charge-reversed mutation-driven T cell responses and inform neoantigen-based ACT development. Structural basis for CD8(+) T cell recognition of the charge-reversed neoantigen UTP20(D2661H).,Wang J, Li S, Mao L, Yang D, Yao Z, Shi J, He W, Wu D J Struct Biol. 2026 Sep 11;218(4):108371. doi: 10.1016/j.jsb.2026.108371. PMID:42727733[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 16:31, 25 September 2026.