{"display":true,"structure":{"allele":{"alpha":{"identifier":"ipd-imgt:HLA34773","locus":"hla-a","match_type":"histo:exact","name":"HLA-A*03:01","slug":"hla_a_03_01","species_stem":"hla"},"beta":{}},"assemblies":{"1":{"assembly_name":"7qpd_1","chains":["B","T","E","M","C","A","D"],"downloaded_at":"2022-11-09T14:41:16.149549"}},"assembly_count":null,"assigned_chains":{"beta2m":{"chains":["B"],"match_type":"histo:assign_chains","score":1.0,"sequence":"IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM"},"calreticulin":{"chains":["C"],"match_type":"histo:assign_chains","score":1.0,"sequence":"EPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL"},"class_i_alpha":{"chains":["M"],"match_type":"histo:assign_chains","score":0.83,"sequence":"GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHEAEQLRAYLDGTCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWELSSQPTIPIVGIIAGLVLLGAVITGAVVAAVMWRRKSSDRKGGSYTQAASSDSAQGSDVSLTACKV"},"erp57":{"chains":["E"],"match_type":"histo:assign_chains","score":1.0,"sequence":"SDVLELTDDNFESRISDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASIVGFFDDSFSEAHSEFLKAASNLRDNYRFAHTNVESLVNEYDDNGEGIILFRPSHLTNKFEDKTVAYTEQKMTSGKIKKFIQENIFGICPHMTEDNKDLIQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGHKLNFAVASRKTFSHELSDFGLESTAGEIPVVAIRTAKGEKFVMQEEFSRDGKALERFLQDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKLNPKKYEGGRELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL"},"tapasin":{"chains":["T"],"match_type":"histo:assign_chains","score":1.0,"sequence":"GPAVIECWFVEDASGKGLAKRPGALLLRQGPGEPPPRPDLDPELYLSVHDPAGALQAAFRRYPRGAPAPHCEMSRFVPLPASAKWASGLTPAQNCPRALDGAWLMVSISSPVLSLSSLLRPQPEPQQEPVLITMATVVLTVLTHTPAPRVRLGQDALLDLSFAYMPPTSEAASSLAPGPPPFGLEWRRQHLGKGHLLLAATPGLNGQMPAAQEGAVAFAAWDDDEPWGPWTGNGTFWLPRVQPFQEGTYLATIHLPYLQGQVTLELAVYKPPKVSLMPATLARAAPGEAPPELLCLVSHFYPSGGLEVEWELRGGPGGRSQKAEGQRWLSALRHHSDGSVSLSGHLQPPPVTTEQHGARYACRIHHPSLPASGRSAEVTLEVAGLSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKKKAE"}},"chronology":{"deposition_date":"2022-01-03","deposition_year":2022,"release_date":"2022-07-20","release_year":2022,"revision_date":"2022-08-24","revision_year":2022},"class":"class_i","classical":true,"complex_type":"class_i_plc","components":["class_i_alpha","beta2m","erp57","tapasin","calreticulin"],"experimental_method":"Electron Microscopy","facets":{},"ligands":[],"locus":"hla-a","manually_edited":{},"missing_residues":[],"page_title":"7QPD | HLA-A*03:01 with Peptide Loading Complex","pdb_code":"7qpd","pdb_title":"Structure of the human MHC i peptide-loading complex editing 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histocompatibility complex class I (MHC I) molecules are central to adaptive immunity. Their assembly, epitope selection, and antigen presentation are controlled by the MHC I glycan through a sophisticated network of chaperones and modifying enzymes. However, the mechanistic integration of the corresponding processes remains poorly understood. Here, we determine the multi-chaperone-client interaction network of the peptide loading complex (PLC) and report the\u00a0PLC editing module structure by cryogenic\u00a0electron microscopy at 3.7\u2009\u00c5 resolution. Combined with epitope-proofreading studies of the PLC in near-native lipid environment, these data show that peptide-receptive MHC I molecules are stabilized by multivalent chaperone interactions including the calreticulin-engulfed mono-glucosylated MHC I glycan, which only becomes accessible for processing by \u03b1-glucosidase II upon loading of optimal epitopes. Our work reveals allosteric coupling between peptide-MHC I assembly and glycan processing. This inter-process communication defines the onset of an adaptive immune response and provides a prototypical example of the tightly coordinated events in endoplasmic reticulum quality control.","bibjson":{"author":[{"initials":"A","lastname":"Domnick","name":"Domnick A"},{"initials":"C","lastname":"Winter","name":"Winter C"},{"initials":"L","lastname":"Su\u0161ac","name":"Su\u0161ac L"},{"initials":"L","lastname":"Hennecke","name":"Hennecke L"},{"initials":"M","lastname":"Hensen","name":"Hensen M"},{"initials":"N","lastname":"Zitzmann","name":"Zitzmann N"},{"initials":"S","lastname":"Trowitzsch","name":"Trowitzsch S"},{"initials":"C","lastname":"Thomas","name":"Thomas C"},{"initials":"R","lastname":"Tamp\u00e9","name":"Tamp\u00e9 R"}],"identifier":[{"id":"10.1038/s41467-022-32384-z","type":"doi"},{"id":"35948544","type":"pubmed"}],"issue":["1"],"journal":{"iso_abbreviation":"Nat Commun","name":""},"pages":["4701"],"title":"Molecular basis of MHC I quality control in the peptide loading complex.","type":"article","url":"https://www.nature.com/articles/s41467-022-32384-z","volume":["13"],"year":[2022]},"in_pmc":"N","in_pmce":"Y","open_access":"Y"},"resolution":"3.73","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/7qpd"},"rcsb":{"url":"https://www.rcsb.org/structure/7qpd"}},"species":{"common_name":"Human","match_type":"histo:assign_species","scientific_name":"Homo sapiens","slug":"homo_sapiens"},"tcr":null,"title":"HLA-A*03:01 with Peptide Loading Complex at 3.73&#8491; resolution","unique_chain_count":5}}
