PubMed:9546397 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/9546397","sourcedb":"PubMed","sourceid":"9546397","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/9546397","text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE 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 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