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Science 22 October 1999:
Vol. 286. no. 5440, pp. 779 - 782
DOI: 10.1126/science.286.5440.779
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Reports

Crystal Structure of the Ectodomain of Human Transferrin Receptor

C. Martin Lawrence, 12 Sanjoy Ray, 1* Marina Babyonyshev, 1 Renate Galluser, 1 David W. Borhani, 1dagger Stephen C. Harrison 12ddagger

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.

1 Howard Hughes Medical Institute and Children's Hospital Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.
2 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
*   Present address: Whitehead Institute, 9 Cambridge Center, Cambridge, MA 02142, USA.

dagger    Present address: Department of Organic Chemistry, 2000 Ninth Avenue South, Southern Research Institute, Birmingham, AL 35205, USA.

ddagger    To whom correspondence should be addressed. E-mail: harrison{at}crystal.harvard.edu

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