Publication Abstract from PubMed
The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome. The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit. One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure. A model is proposed for Tf binding to the receptor.
Crystal structure of the ectodomain of human transferrin receptor.,Lawrence CM, Ray S, Babyonyshev M, Galluser R, Borhani DW, Harrison SC Science. 1999 Oct 22;286(5440):779-82. PMID:10531064[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
