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X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors

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  • Thorsten Althoff

    (Vollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA
    Present addresses: Department of Physiology, David Geffen School of Medicine, University of California Los Angeles, 10833 Le Conte Avenue, Los Angeles, California 90095-1751, USA (T.A.); Department of Neuroscience, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, Texas 75390-9111, USA (R.E.H.).)

  • Ryan E. Hibbs

    (Vollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA
    Present addresses: Department of Physiology, David Geffen School of Medicine, University of California Los Angeles, 10833 Le Conte Avenue, Los Angeles, California 90095-1751, USA (T.A.); Department of Neuroscience, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, Texas 75390-9111, USA (R.E.H.).)

  • Surajit Banerjee

    (NE-CAT/Cornell University, 9700 South Cass Avenue, Building 436 E001, Argonne, Illinois 60439, USA)

  • Eric Gouaux

    (Vollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA
    Howard Hughes Medical Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA)

Abstract

This study solved structures of the glutamate-gated chloride channel (GluCl), a Cys-loop receptor from C. elegans, in an apo, closed state and in a lipid-bound state — comparison of these structures with a previously published structure of GluCl in an ivermectin-bound state reveals what conformational changes probably occur as this membrane protein transitions from the closed/resting state towards an open/activated state.

Suggested Citation

  • Thorsten Althoff & Ryan E. Hibbs & Surajit Banerjee & Eric Gouaux, 2014. "X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors," Nature, Nature, vol. 512(7514), pages 333-337, August.
    • Handle: RePEc:nat:nature:v:512:y:2014:i:7514:d:10.1038_nature13669
    DOI: 10.1038/nature13669
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    Cited by:

    1. Dagimhiwat H. Legesse & Chen Fan & Jinfeng Teng & Yuxuan Zhuang & Rebecca J. Howard & Colleen M. Noviello & Erik Lindahl & Ryan E. Hibbs, 2023. "Structural insights into opposing actions of neurosteroids on GABAA receptors," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Peng Huang & Raminta Venskutonytė & Rashmi B. Prasad & Hamidreza Ardalani & Sofia W. Maré & Xiao Fan & Ping Li & Peter Spégel & Nieng Yan & Pontus Gourdon & Isabella Artner & Karin Lindkvist-Petersso, 2023. "Cryo-EM structure supports a role of AQP7 as a junction protein," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Shingo Hiroki & Hikari Yoshitane & Hinako Mitsui & Hirofumi Sato & Chie Umatani & Shinji Kanda & Yoshitaka Fukada & Yuichi Iino, 2022. "Molecular encoding and synaptic decoding of context during salt chemotaxis in C. elegans," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    4. John T. Petroff & Noah M. Dietzen & Ezry Santiago-McRae & Brett Deng & Maya S. Washington & Lawrence J. Chen & K. Trent Moreland & Zengqin Deng & Michael Rau & James A. J. Fitzpatrick & Peng Yuan & Th, 2022. "Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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