Structural and functional studies on the stalk of the transferrin receptor

Danijela Dukovski, Zongli Li, Deb Kelly, Eric Mack, Thomas Walz

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Transferrin (Tf) is an iron carrier protein that consists of two lobes, the N- and C-lobes, which can each bind a Fe3+ ion. Tf binds to its receptor (TfR), which mediates iron delivery to cells through an endocytotic pathway. Receptor binding facilitates iron release from the Tf C-lobe, but impedes iron release from the N-lobe. An atomic model of the Tf-TfR complex based on single particle electron microscopy (EM) indicated that receptor binding is indeed likely to hinder opening of the N-lobe, thus interfering with its iron release. The atomic model also suggested that the TfR stalks could form additional contacts with the Tf N-lobes, thus potentially further slowing down its iron release. Here, we show that the TfR stalks are unlikely to make strong interactions with the Tf N-lobes and that the stalks have no effect on iron release from the N-lobes of receptor-bound Tf.

Original languageEnglish (US)
Pages (from-to)712-716
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume381
Issue number4
DOIs
StatePublished - Apr 17 2009

Fingerprint

Transferrin Receptors
Transferrin
Iron
Electron microscopy
Electron Microscopy
Carrier Proteins
Ions

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Dukovski, Danijela ; Li, Zongli ; Kelly, Deb ; Mack, Eric ; Walz, Thomas. / Structural and functional studies on the stalk of the transferrin receptor. In: Biochemical and Biophysical Research Communications. 2009 ; Vol. 381, No. 4. pp. 712-716.
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Structural and functional studies on the stalk of the transferrin receptor. / Dukovski, Danijela; Li, Zongli; Kelly, Deb; Mack, Eric; Walz, Thomas.

In: Biochemical and Biophysical Research Communications, Vol. 381, No. 4, 17.04.2009, p. 712-716.

Research output: Contribution to journalArticle

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