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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Structure of the human transferrin receptor-transferrin complex.

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  • 1Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.

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Researchers visualized the transferrin receptor-transferrin complex using cryo-electron microscopy. This structural insight explains how transferrin (Tf) binding to the transferrin receptor (TfR) facilitates cellular iron uptake.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Iron is essential for cellular function but toxic in free form.
  • Transferrin (Tf) transports iron (Fe3+) throughout the body.
  • Cellular iron uptake occurs via endocytosis of the transferrin receptor (TfR)-Tf complex.

Purpose of the Study:

  • To elucidate the molecular details of transferrin receptor-transferrin complex formation.
  • To provide a high-resolution structural model of the TfR-Tf complex.

Main Methods:

  • Cryo-electron microscopy was used to generate a subnanometer resolution density map.
  • Atomic models were created by fitting crystal structures of diferric Tf and the TfR ectodomain into the map.

Main Results:

  • The N-lobe of Tf is positioned between the membrane and the TfR ectodomain.
  • The C-lobe of Tf abuts the receptor's helical domain.
  • Tf binding induces a conformational change in Tf, with its N-lobe moving ~9 Å relative to the C-lobe.

Conclusions:

  • The determined structure provides a molecular basis for TfR-Tf complex formation.
  • This structural understanding helps explain differences in iron release between free and receptor-bound Tf.
  • The findings offer insights into the mechanism of cellular iron delivery.