{"display":true,"structure":{"allele":{"alpha":{"identifier":"uniprot:P01901","locus":"h2-k","match_type":"histo:fuzzy","name":"H2-Kb","slug":"h2_kb","species_stem":"H2"},"beta":{}},"assemblies":{"1":{"assembly_name":"1a6z_1","chains":["A","B"],"downloaded_at":"2022-11-09T14:44:13.954750"},"2":{"assembly_name":"1a6z_2","chains":["C","D"],"downloaded_at":"2022-11-09T14:44:14.325783"}},"assembly_count":null,"assigned_chains":{"beta2m":{"chains":["B","D"],"match_type":"histo:assign_chains","score":1.0,"sequence":"IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM"},"hfe2":{"chains":["A","C"],"match_type":"histo:assign_chains","score":1.0,"sequence":"RLLRSHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDHESRRVEPRTPWVSSRISSQMWLQLSQSLKGWDHMFTVDFWTIMENHNHSKESHTLQVILGCEMQEDNSTEGYWKYGYDGQDHLEFCPDTLDWRAAEPRAWPTKLEWERHKIRARQNRAYLERDCPAQLQQLLELGRGVLDQQVPPLVKVTHHVTSSVTTLRCRALNYYPQNITMKWLKDKQPMDAKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQVEHPGLDQPLIVIW"}},"chronology":{"deposition_date":"1998-03-04","deposition_year":1998,"release_date":"1999-03-23","release_year":1999,"revision_date":"2011-07-13","revision_year":2011},"class":"class_i","classical":false,"complex_type":"hfe2","components":["hfe2","beta2m"],"experimental_method":"X-ray diffraction","facets":{},"ligands":[],"locus":"h2-k","manually_edited":{},"missing_residues":[],"page_title":"1A6Z | Non-classical MHC Class I molecule haemochromatosis protein (HFE)","pdb_code":"1a6z","pdb_title":"Hfe (human) hemochromatosis protein","peptide":{"actual_sequence":null,"epitope_info":{},"features":[],"full_sequence":null,"gap_info":{},"gapped_sequence":null,"length":{"numeric":null,"text":null},"unnatural_amino_acids":[]},"publication":{"abstract":"HFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex.","bibjson":{"author":[{"initials":"JA","lastname":"Lebr\ufffd\ufffdn","name":"Lebr\ufffd\ufffdn JA"},{"initials":"MJ","lastname":"Bennett","name":"Bennett MJ"},{"initials":"DE","lastname":"Vaughn","name":"Vaughn DE"},{"initials":"AJ","lastname":"Chirino","name":"Chirino AJ"},{"initials":"PM","lastname":"Snow","name":"Snow PM"},{"initials":"GA","lastname":"Mintier","name":"Mintier GA"},{"initials":"JN","lastname":"Feder","name":"Feder JN"},{"initials":"PJ","lastname":"Bjorkman","name":"Bjorkman PJ"}],"identifier":[{"id":"10.1016/s0092-8674(00)81151-4","type":"doi"},{"id":"9546397","type":"pubmed"}],"issue":["1"],"journal":{"iso_abbreviation":"Cell","name":""},"pages":["111-23"],"title":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.","type":"article","url":"https://www.sciencedirect.com/science/article/abs/pii/S0092867400811514","volume":["93"],"year":[1998]},"in_pmc":"N","in_pmce":"N","open_access":"N"},"resolution":"2.60","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/1a6z"},"rcsb":{"url":"https://www.rcsb.org/structure/1a6z"}},"species":{"common_name":"Human","match_type":"histo:assign_species","scientific_name":"Homo sapiens","slug":"homo_sapiens"},"tcr":null,"title":"Non-classical MHC Class I molecule haemochromatosis protein (HFE) at 2.60Å resolution","unique_chain_count":2}}