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. 2023 Nov 17;14:1303304. doi: 10.3389/fimmu.2023.1303304

Table 1.

Structures of TCR–pMHC complexes involving cancer neoantigens.

TCR–pMHC complex PDB code (reference) Neoepitope Affinity
wild-type      
Affinity
mutant
Basis for neoepitope immunogenicity
E8–TPIT28I–HLA-DR1 2IAM (18) GELIGILNAAKVPAD UD >300 μM Direct TCR contacts with mutation
G4–TPIT28I–HLA-DR1 4E41 (19) GELIGILNAAKVPAD UD >300 μM Direct TCR contacts with mutation
12-6–p53R175H–HLA-A*02:01 6VRM (20) HMTEVVRHC UD 1.1 μM Direct TCR contacts with mutation
38-10–p53R175H–HLA-A*02:01 6VRN (20) HMTEVVRHC UD 39.9 μM Direct TCR contacts with mutation
1a2–p53R175H–HLA-A*02:01 6VQO (20) HMTEVVRHC UD 16.2 μM Direct TCR contacts with mutation
6-11–p53R175H–HLA-A*02:01 7RM4 (21) HMTEVVRHC 214 μM 3.5 μM No direct TCR contacts with mutation
Reduced energetic cost of desolvating mutation during TCR engagement
9a–KRASG12D–HLA-C*08:02 6ULN (22) GADGVGKSA NA 16 nM Stabilization of pMHC ligand by anchor residue mutation
9d–KRASG12D–HLA-C*08:02 6ULR (22) GADGVGKSA NA 125 nM Stabilization of pMHC ligand by anchor residue mutation
10–KRASG12D–HLA-C*08:02 6UON (22) GADGVGKSAL NA 6.7 μM Stabilization of pMHC ligand by anchor residue mutation
JDI–KRASG12D–HLA-C*11:01 7PB2 (23) VVVGADGVGK UD 63 μM No direct TCR contacts with mutation
Formation of new electrostatic interactions of mutant peptide with TCR
1-2C–KRASG12V–HLA-A*11*01 8I5C (24) VVGAVGVGK 131 μM 14 μM Direct TCR contacts with mutation
3-2E–KRASG12V–HLA-A*11*01 8I5D (24) VVGAVGVGK 42 μM 28 μM Direct TCR contacts with mutation
302TIL–HHATp8F–HLA-A*02:06 6UK4 (25) KQWLVWLFL 200 μM 9 μM Conformational pre-organization of pMHC ligand by mutation
3–PIK3CAH1047L–HLA-A*03:01 7RRG (26) ALHGGWTTK ND 200 μM Stabilization of pMHC ligand by anchor residue mutation
4–PIK3CAH1047L–HLA-A*03:01 7L1D (26) ALHGGWTTK ND 49 μM Stabilization of pMHC ligand by anchor residue mutation

UD, undetectable; NA, not applicable; ND, not determined.