Crystal Structure of the Ectodomain of Human Transferrin Receptor
Author:
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
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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