PubMed:10638746 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/10638746","sourcedb":"PubMed","sourceid":"10638746","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/10638746","text":"Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor.\nHFE is related to major histocompatibility complex (MHC) class I proteins and is mutated in the iron-overload disease hereditary haemochromatosis. HFE binds to the transferrin receptor (TfR), a receptor by which cells acquire iron-loaded transferrin. The 2.8 A crystal structure of a complex between the extracellular portions of HFE and TfR shows two HFE molecules which grasp each side of a twofold symmetric TfR dimer. On a cell membrane containing both proteins, HFE would 'lie down' parallel to the membrane, such that the HFE helices that delineate the counterpart of the MHC peptide-binding groove make extensive contacts with helices in the TfR dimerization domain. The structures of TfR alone and complexed with HFE differ in their domain arrangement and dimer interfaces, providing a mechanism for communicating binding events between TfR chains. The HFE-TfR complex suggests a binding site for transferrin on TfR and sheds light upon the function of HFE in regulating iron 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