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Crystal structure of the human thioredoxin reductase–thioredoxin complex

Author

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  • Karin Fritz-Wolf

    (Interdisciplinary Research Centre, Justus Liebig University
    Max Planck Institute for Medical Research)

  • Sebastian Kehr

    (Interdisciplinary Research Centre, Justus Liebig University)

  • Michaela Stumpf

    (Interdisciplinary Research Centre, Justus Liebig University)

  • Stefan Rahlfs

    (Interdisciplinary Research Centre, Justus Liebig University)

  • Katja Becker

    (Interdisciplinary Research Centre, Justus Liebig University)

Abstract

Thioredoxin reductase 1 (TrxR1) is a homodimeric flavoprotein crucially involved in the regulation of cellular redox homeostasis, growth, and differentiation. Its importance in various diseases makes TrxR1 a highly interesting drug target. Here we present the first crystal structures of human TrxR1 in complex with its substrate thioredoxin (Trx). The carboxy-terminal redox centre is found about 20 Å apart from the amino-terminal redox centre, with no major conformational changes in TrxR or Trx. Thus, our structure confirms that the enzyme uses a flexible C-terminal arm for electron transport to its substrates, which is stabilized by a guiding bar for controlled transfer. This notion is supported by mutational analyses. Furthermore, essential residues of the interface region were characterized both structurally and functionally. The structure provides templates for future drug design, and contributes to our understanding of redox regulatory processes in mammals.

Suggested Citation

  • Karin Fritz-Wolf & Sebastian Kehr & Michaela Stumpf & Stefan Rahlfs & Katja Becker, 2011. "Crystal structure of the human thioredoxin reductase–thioredoxin complex," Nature Communications, Nature, vol. 2(1), pages 1-8, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1382
    DOI: 10.1038/ncomms1382
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