report an affinity‐enhanced TCR that recognizes KRAS‐G12D in the context of HLA‐A*11:01, but this TCR also exhibited substantial cross‐binding to the wildtype KRAS peptide.[18] Furthermore, a TCR with excessively strong binding affinity may lead to early exhaustion of the T cells upon engagement with target cells, dampening the anti‐tumor immunity.[19, 20] Therefore, engineering soluble TCR engagers with TCRs of physiological affinity holds substantial clinical significance for TCR‐based drug design. The gene discussed is HLA-A; the disease is neoplasm.