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The cryo-electron microscopy structure of human transcription factor IIH

Author

Listed:
  • Basil J. Greber

    (California Institute for Quantitative Biology (QB3), University of California
    Lawrence Berkeley National Laboratory)

  • Thi Hoang Duong Nguyen

    (California Institute for Quantitative Biology (QB3), University of California
    Lawrence Berkeley National Laboratory
    Miller Institute for Basic Research in Science, University of California)

  • Jie Fang

    (Howard Hughes Medical Institute, University of California)

  • Pavel V. Afonine

    (Lawrence Berkeley National Laboratory)

  • Paul D. Adams

    (Lawrence Berkeley National Laboratory
    University of California)

  • Eva Nogales

    (California Institute for Quantitative Biology (QB3), University of California
    Lawrence Berkeley National Laboratory
    Howard Hughes Medical Institute, University of California
    University of California)

Abstract

The cryo-electron microscopy structure of the ten-subunit human transcription factor IIH, revealing the molecular architecture of the TFIIH core complex, the detailed structures of its constituent XPB and XPD ATPases, and how the core and kinase subcomplexes of TFIIH are connected.

Suggested Citation

  • Basil J. Greber & Thi Hoang Duong Nguyen & Jie Fang & Pavel V. Afonine & Paul D. Adams & Eva Nogales, 2017. "The cryo-electron microscopy structure of human transcription factor IIH," Nature, Nature, vol. 549(7672), pages 414-417, September.
    • Handle: RePEc:nat:nature:v:549:y:2017:i:7672:d:10.1038_nature23903
    DOI: 10.1038/nature23903
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    Cited by:

    1. Jina Yu & Chunli Yan & Thomas Dodd & Chi-Lin Tsai & John A. Tainer & Susan E. Tsutakawa & Ivaylo Ivanov, 2023. "Dynamic conformational switching underlies TFIIH function in transcription and DNA repair and impacts genetic diseases," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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