Structural highlights
Function
Q53Z42_HUMAN Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364]
Publication Abstract from PubMed
Major histocompatibility complex (MHC) proteins present peptides on the cell surface for T cell surveillance. Reliable in silico prediction of which peptides would be presented and which T cell receptors would recognize them is an important problem in structural immunology. Here, we introduce an AlphaFold-based pipeline for predicting the three-dimensional structures of peptide-MHC complexes for class I and class II MHC molecules. Our method demonstrates high accuracy, outperforming existing tools in class I modeling accuracy and class II peptide register prediction. We validate its performance and utility with new experimental data on a recently described cancer neoantigen/wild-type peptide pair and explore applications toward improving peptide-MHC binding prediction.
Accurate modeling of peptide-MHC structures with AlphaFold.,Mikhaylov V, Brambley CA, Keller GLJ, Arbuiso AG, Weiss LI, Baker BM, Levine AJ Structure. 2023 Dec 14:S0969-2126(23)00413-6. doi: 10.1016/j.str.2023.11.011. PMID:38113889[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mikhaylov V, Brambley CA, Keller GLJ, Arbuiso AG, Weiss LI, Baker BM, Levine AJ. Accurate modeling of peptide-MHC structures with AlphaFold. Structure. 2023 Dec 14:S0969-2126(23)00413-6. PMID:38113889 doi:10.1016/j.str.2023.11.011
