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Multidomain integration in the structure of the HNF-4α nuclear receptor complex

Author

Listed:
  • Vikas Chandra

    (Metabolic Signaling and Disease Program, Sanford-Burnham Medical Research Institute)

  • Pengxiang Huang

    (Metabolic Signaling and Disease Program, Sanford-Burnham Medical Research Institute)

  • Nalini Potluri

    (Metabolic Signaling and Disease Program, Sanford-Burnham Medical Research Institute)

  • Dalei Wu

    (Metabolic Signaling and Disease Program, Sanford-Burnham Medical Research Institute)

  • Youngchang Kim

    (Structural Biology Center, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, Illinois 60439, USA)

  • Fraydoon Rastinejad

    (Metabolic Signaling and Disease Program, Sanford-Burnham Medical Research Institute)

Abstract

The crystal structure of the transcriptional regulator HNF-4α bound to its DNA response element and coactivator-derived peptides is described, revealing a multidomain convergence centre that serves as an allosteric transmission system.

Suggested Citation

  • Vikas Chandra & Pengxiang Huang & Nalini Potluri & Dalei Wu & Youngchang Kim & Fraydoon Rastinejad, 2013. "Multidomain integration in the structure of the HNF-4α nuclear receptor complex," Nature, Nature, vol. 495(7441), pages 394-398, March.
    • Handle: RePEc:nat:nature:v:495:y:2013:i:7441:d:10.1038_nature11966
    DOI: 10.1038/nature11966
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    Cited by:

    1. Natasha Hui Jin Ng & Soumita Ghosh & Chek Mei Bok & Carmen Ching & Blaise Su Jun Low & Juin Ting Chen & Euodia Lim & María Clara Miserendino & Yaw Sing Tan & Shawn Hoon & Adrian Kee Keong Teo, 2024. "HNF4A and HNF1A exhibit tissue specific target gene regulation in pancreatic beta cells and hepatocytes," Nature Communications, Nature, vol. 15(1), pages 1-21, December.

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