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The chaperones Tapasin (Tsn) and TAP-binding protein-related (TAPBPR) facilitate MHC I peptide loading and high-affinity epitope selection. Despite the pivotal role of Tsn and TAPBPR in controlling the hierarchical immune response, their catalytic mechanism remains unknown. Here, we present the x-ray structure of the TAPBPR-MHC I complex, which delineates the central step of catalysis. TAPBPR functions as peptide selector by remodeling the MHC I \u03b12-1-helix region, stabilizing the empty binding groove, and inserting a loop into the groove that interferes with peptide binding. The complex explains how mutations in MHC I-specific chaperones cause defects in antigen processing and suggests a unifying mechanism of peptide proofreading.","bibjson":{"author":[{"initials":"C","lastname":"Thomas","name":"Thomas C"},{"initials":"R","lastname":"Tamp\u00e9","name":"Tamp\u00e9 R"}],"identifier":[{"id":"10.1126/science.aao6001","type":"doi"},{"id":"29025996","type":"pubmed"}],"issue":[null],"journal":{"iso_abbreviation":"Science","name":""},"pages":[null],"title":"Structure of the TAPBPR-MHC I complex defines the mechanism of peptide loading and editing.","type":"article","url":"https://www.sciencemag.org/lookup/doi/10.1126/science.aao6001","volume":[null],"year":[2017]},"in_pmc":"N","in_pmce":"N","open_access":"N"},"resolution":"3.30","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/5opi"},"rcsb":{"url":"https://www.rcsb.org/structure/5opi"}},"species":{"common_name":"Mouse","match_type":"histo:assign_species","scientific_name":"Mus musculus","slug":"mus_musculus"},"tcr":null,"title":"H2-Db with peptide editor TAPBPR at 3.30Å resolution","unique_chain_count":3}}