http://purl.uniprot.org/citations/10638746 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10638746 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10638746 | http://www.w3.org/2000/01/rdf-schema#comment | "HFE 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 homeostasis."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.org/dc/terms/identifier | "doi:10.1038/47417"xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.org/dc/terms/identifier | "doi:10.1038/47417"xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/author | "Bennett M.J."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/author | "Bennett M.J."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/author | "Bjorkman P.J."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/author | "Bjorkman P.J."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/author | "Lebron J.A."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/author | "Lebron J.A."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/pages | "46-53"xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/pages | "46-53"xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/title | "Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/title | "Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor."xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/volume | "403"xsd:string |
http://purl.uniprot.org/citations/10638746 | http://purl.uniprot.org/core/volume | "403"xsd:string |
http://purl.uniprot.org/citations/10638746 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10638746 |
http://purl.uniprot.org/citations/10638746 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10638746 |
http://purl.uniprot.org/citations/10638746 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10638746 |
http://purl.uniprot.org/citations/10638746 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10638746 |