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Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3

Author

Listed:
  • Stefan Schoebel

    (Harvard Medical School
    University of Gothenburg)

  • Wei Mi

    (Harvard Medical School)

  • Alexander Stein

    (Max Planck Institute for Biophysical Chemistry)

  • Sergey Ovchinnikov

    (Institute for Protein Design, University of Washington)

  • Ryan Pavlovicz

    (Institute for Protein Design, University of Washington)

  • Frank DiMaio

    (Institute for Protein Design, University of Washington)

  • David Baker

    (Institute for Protein Design, University of Washington)

  • Melissa G. Chambers

    (Harvard Medical School)

  • Huayou Su

    (National Lab for Parallel and Distributed Processing (PDL), School of Computer Science, National University of Defense Technology)

  • Dongsheng Li

    (National Lab for Parallel and Distributed Processing (PDL), School of Computer Science, National University of Defense Technology)

  • Tom A. Rapoport

    (Harvard Medical School)

  • Maofu Liao

    (Harvard Medical School)

Abstract

The structure of yeast Hrd1 in complex with Hrd3 shows that Hrd1 forms an aqueous cavity with a lateral seal within the endoplasmic reticulum membrane, shedding light on how misfolded proteins are transported out of the endoplasmic reticulum.

Suggested Citation

  • Stefan Schoebel & Wei Mi & Alexander Stein & Sergey Ovchinnikov & Ryan Pavlovicz & Frank DiMaio & David Baker & Melissa G. Chambers & Huayou Su & Dongsheng Li & Tom A. Rapoport & Maofu Liao, 2017. "Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3," Nature, Nature, vol. 548(7667), pages 352-355, August.
    • Handle: RePEc:nat:nature:v:548:y:2017:i:7667:d:10.1038_nature23314
    DOI: 10.1038/nature23314
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    Cited by:

    1. Liangguang Leo Lin & Huilun Helen Wang & Brent Pederson & Xiaoqiong Wei & Mauricio Torres & You Lu & Zexin Jason Li & Xiaodan Liu & Hancheng Mao & Hui Wang & Linyao Elina Zhou & Zhen Zhao & Shengyi Su, 2024. "SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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