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Structural basis of kainate subtype glutamate receptor desensitization

Author

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  • Joel R. Meyerson

    (Laboratory of Cell Biology, Center for Cancer Research, NCI, NIH, Bethesda
    †Present address: Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA.)

  • Sagar Chittori

    (Laboratory of Cell Biology, Center for Cancer Research, NCI, NIH, Bethesda
    Laboratory of Cellular and Molecular Neurophysiology, Porter Neuroscience Research Center, NICHD, NIH)

  • Alan Merk

    (Laboratory of Cell Biology, Center for Cancer Research, NCI, NIH, Bethesda)

  • Prashant Rao

    (Laboratory of Cell Biology, Center for Cancer Research, NCI, NIH, Bethesda)

  • Tae Hee Han

    (Program in Cellular Regulation and Metabolism, NICHD, NIH)

  • Mihaela Serpe

    (Program in Cellular Regulation and Metabolism, NICHD, NIH)

  • Mark L. Mayer

    (Laboratory of Cellular and Molecular Neurophysiology, Porter Neuroscience Research Center, NICHD, NIH)

  • Sriram Subramaniam

    (Laboratory of Cell Biology, Center for Cancer Research, NCI, NIH, Bethesda)

Abstract

The high-resolution cryo-electron microscopy structure of the kainate receptor GluK2 subtype in its desensitized state is reported, which reveals that desensitization is attained by establishing a ring-like structure in the ligand-binding domains.

Suggested Citation

  • Joel R. Meyerson & Sagar Chittori & Alan Merk & Prashant Rao & Tae Hee Han & Mihaela Serpe & Mark L. Mayer & Sriram Subramaniam, 2016. "Structural basis of kainate subtype glutamate receptor desensitization," Nature, Nature, vol. 537(7621), pages 567-571, September.
    • Handle: RePEc:nat:nature:v:537:y:2016:i:7621:d:10.1038_nature19352
    DOI: 10.1038/nature19352
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    Cited by:

    1. Shanti Pal Gangwar & Maria V. Yelshanskaya & Muhammed Aktolun & Laura Y. Yen & Thomas P. Newton & Kristian Strømgaard & Maria G. Kurnikova & Alexander I. Sobolevsky, 2024. "Trapping of spermine, Kukoamine A, and polyamine toxin blockers in GluK2 kainate receptor channels," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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