Structural basis of kainate subtype glutamate receptor desensitization

Joel R. Meyerson (), Sagar Chittori, Alan Merk, Prashant Rao, Tae Hee Han, Mihaela Serpe, Mark L. Mayer () and Sriram Subramaniam ()
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Joel R. Meyerson: Laboratory of Cell Biology, Center for Cancer Research, NCI, NIH, Bethesda
Sagar Chittori: Laboratory of Cell Biology, Center for Cancer Research, NCI, NIH, Bethesda
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

Nature, 2016, vol. 537, issue 7621, 567-571

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.

Date: 2016
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DOI: 10.1038/nature19352

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