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to CD8<sup>+</sup> T cell-mediated immunity is the recognition of peptide-major histocompatibility complex class I (p-MHC I) proteins displayed by antigen-presenting cells. Chaperone-mediated loading of high-affinity peptides onto MHC I is a key step in the MHC I antigen presentation pathway. However, the structure of MHC I with a chaperone that facilitates peptide loading has not been determined. We report the crystal structure of MHC I in complex with the peptide editor TAPBPR (TAP-binding protein-related), a tapasin homolog. TAPBPR remodels the peptide-binding groove of MHC I, resulting in the release of low-affinity peptide. Changes include groove relaxation, modifications of key binding pockets, and domain adjustments. This structure captures a peptide-receptive state of MHC I and provides insights into the mechanism of peptide editing by TAPBPR and, by analogy, tapasin.","bibjson":{"author":[{"initials":"J","lastname":"Jiang","name":"Jiang J"},{"initials":"K","lastname":"Natarajan","name":"Natarajan K"},{"initials":"LF","lastname":"Boyd","name":"Boyd LF"},{"initials":"GI","lastname":"Morozov","name":"Morozov GI"},{"initials":"MG","lastname":"Mage","name":"Mage MG"},{"initials":"DH","lastname":"Margulies","name":"Margulies DH"}],"identifier":[{"id":"10.1126/science.aao5154","type":"doi"},{"id":"29025991","type":"pubmed"}],"issue":[null],"journal":{"iso_abbreviation":"Science","name":""},"pages":[null],"title":"Crystal structure of a TAPBPR-MHC-I complex reveals the mechanism of peptide editing in antigen presentation.","type":"article","url":"https://www.sciencemag.org/lookup/doi/10.1126/science.aao5154","volume":[null],"year":[2017]},"in_pmc":"N","in_pmce":"Y","open_access":"N"},"resolution":"3.41","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/5wer"},"rcsb":{"url":"https://www.rcsb.org/structure/5wer"}},"species":{"common_name":"Mouse","match_type":"histo:assign_species","scientific_name":"Mus musculus","slug":"mus_musculus"},"tcr":null,"title":"H2-Dd with peptide editor TAPBPR at 3.41&#8491; resolution","unique_chain_count":3}}