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K2P2.1 (TREK-1)–activator complexes reveal a cryptic selectivity filter binding site

Author

Listed:
  • Marco Lolicato

    (Cardiovascular Research Institute, University of California)

  • Cristina Arrigoni

    (Cardiovascular Research Institute, University of California)

  • Takahiro Mori

    (Ono Pharmaceutical Co. Ltd)

  • Yoko Sekioka

    (Ono Pharmaceutical Co. Ltd)

  • Clifford Bryant

    (Small Molecule Discovery Center, University of California)

  • Kimberly A. Clark

    (Cardiovascular Research Institute, University of California)

  • Daniel L. Minor

    (Cardiovascular Research Institute, University of California
    and Cellular and Molecular Pharmacology, University of California
    California Institute for Quantitative Biomedical Research, University of California
    Kavli Institute for Fundamental Neuroscience, University of California)

Abstract

Crystal structures of an activated two-pore potassium channel reveal a cryptic binding pocket that binds small-molecule activators that restrict the mobility of the selectivity filter and surrounding structure, stabilizing an active ‘leak-mode’ conformation.

Suggested Citation

  • Marco Lolicato & Cristina Arrigoni & Takahiro Mori & Yoko Sekioka & Clifford Bryant & Kimberly A. Clark & Daniel L. Minor, 2017. "K2P2.1 (TREK-1)–activator complexes reveal a cryptic selectivity filter binding site," Nature, Nature, vol. 547(7663), pages 364-368, July.
    • Handle: RePEc:nat:nature:v:547:y:2017:i:7663:d:10.1038_nature22988
    DOI: 10.1038/nature22988
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