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Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel

Author

Listed:
  • Ji She

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Jiangtao Guo

    (Zhejiang University School of Medicine)

  • Qingfeng Chen

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

  • Weizhong Zeng

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

  • Youxing Jiang

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

  • Xiao-chen Bai

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

Abstract

Structures of the voltage-gated and phosphatidylinositol 3,5-bisphosphate-activated mouse two-pore channel TPC1 in apo and ligand-bound states provide insights into the selectivity and gating mechanisms of mammalian two-pore channels.

Suggested Citation

  • Ji She & Jiangtao Guo & Qingfeng Chen & Weizhong Zeng & Youxing Jiang & Xiao-chen Bai, 2018. "Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel," Nature, Nature, vol. 556(7699), pages 130-134, April.
    • Handle: RePEc:nat:nature:v:556:y:2018:i:7699:d:10.1038_nature26139
    DOI: 10.1038/nature26139
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