9xme | pdb_00009xme

Complex of HLA-A2, a class I MHC, with a wild type UTP20 peptide

spinqualitylabelsall models 9xme, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9xme is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.04Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8WLS4_HUMAN Publication Abstract from PubMed Adoptive 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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