Crystal Structure of the Ectodomain of Human Transferrin Receptor-Reference-Cited by-同舟云学术

Crystal Structure of the Ectodomain of Human Transferrin Receptor

Published:1999-10-22 Issue:5440 Volume:286 Page:779-782
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Lawrence C. Martin¹²,Ray Sanjoy¹,Babyonyshev Marina¹,Galluser Renate¹,Borhani David W.¹,Harrison Stephen C.¹²

Affiliation:

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.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference46 articles.

1. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells

2. Abbreviations for amino acid residues are as follows: A Ala; C Cys; D Asp; E Glu; F Phe; G Gly; H His; I Ile; K Lys; L Leu; M Met; N Asn; P Pro; Q Gln; R Arg; S Ser; T Thr; V Val; W Trp; Y Tyr.

3. Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

4. Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin receptor

5. Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site.

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