Experimental structures of antibody/MHC-I complexes reveal details of epitopes overlooked by computational prediction.

ABSTRACT: Monoclonal antibodies (mAb) to major histocompatibility complex class I (MHC-I) molecules have proved to be crucial reagents for tissue typing and fundamental studies of immune recognition. To augment our understanding of epitopic sites seen by a set of anti-MHC-I mAb, we determined X-ray crystal structures of four complexes of anti-MHC-I antigen-binding fragments (Fab) bound to peptide/MHC-I/β₂m (pMHC-I). An anti-H2-D^d mAb, two anti-MHC-I α3 domain mAb, and an anti-β₂-microglobulin (β₂m) mAb bind pMHC-I at sites consistent with earlier mutational and functional experiments, and the structures explain allelomorph specificity. Comparison of the experimentally determined structures with computationally derived models using AlphaFold Multimer (AF-M)

SUBMITTER: Boyd LF 

PROVIDER: S-EPMC10723347 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature