Phosphorylation of a tumor-derived ASXL2 epitope remodels 1 peptide-HLA binding affinity and interaction dynamics
This study demonstrates that phosphorylation of a tumor-derived ASXL2 epitope enhances its binding affinity to HLA class I molecules by reconfiguring non-bonded interaction networks and altering the complex's conformational dynamics, thereby providing a structural basis for targeting such post-translationally modified epitopes in cancer immunotherapy.