Cited by 315Iron Metabolism and DisordersEnzyme Structure and FunctionCellular transport and secretion

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Crystal Structure of the Ectodomain of Human Transferrin Receptor

Lawrence, C. Martin, Ray, Sanjoy, Babyonyshev, Marina, Galluser, Renate, Borhani, David W., Harrison, Stephen C.·1999·Science

DOI 10.1126/science.286.5440.779

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Abstract

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.

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10.1182/blood.V83.2.580.580 · DOI
J. N. Feder et al. Proc. Natl. Acad. Sci. U.S.A. 95 1472 (1998)
Letters A to H designate the eight TfR monomers in the crystallographic asymmetric unit. The physiological dimers were identified by the proximity of their NH 2 -termini. They are the four pairs AB CD EF and GH related to each other by the 8 5 noncrystallographic symmetry. Each dimer interface has a large solvent-inaccessible surface area of 4100 Å 2 . There are also significant contacts between successive dimers within the 8 5 helical columns (2600 Å 2 ).
Supplementary material is available at www.sciencemag.org/feature/data/1043272.shl
A. T. Brunger X-PLOR Version 3.0: A System for Crystallography and NMR (Yale University Press New Haven CT 1992).

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Authors: Lawrence, C. M., Ray, S., Babyonyshev, M., Galluser, R., Borhani, D. W., & Harrison, S. C.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: Ray, Sanjoy
Borhani, David W.
Harrison, Stephen C.
ORCID: Lawrence, C. Martin
Borhani, David W.
Harrison, Stephen C.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1999-10-22
Volume: 286
Issue: 5440
Pages: 779-782
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.286.5440.779
OpenAlex: W2167563458
Cited by: 315
References: 38
Citations by year: 2026: 6 · 2025: 9 · 2024: 13 · 2023: 13 · 2022: 10 · 2021: 4 · 2020: 15 · 2019: 14 · 2018: 9 · 2017: 5 · 2016: 7 · 2015: 5 · 2014: 7 · 2013: 5 · 2012: 11
FWCI: 7.86
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: transferrin receptor, extracellular domain, crystal structure, clathrin-mediated endocytosis, transferrin binding, iron imports, receptor dimer
MeSH terms: Amino Acid Sequence, Animals, Carboxypeptidases, Cell Membrane, Ferric Compounds, Glycosylation, Cricetinae, Humans, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Conformation, Receptors, Transferrin, Transferrin, CHO Cells, Conserved Sequence, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Dimerization

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Crystal Structure of the Ectodomain of Human Transferrin Receptor

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