Crystal structure and association behaviour of the GluR2 amino‐terminal domain |
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| Authors: | Rongsheng Jin Satinder K Singh Shenyan Gu Hiroyasu Furukawa Alexander I Sobolevsky Jie Zhou Yan Jin Eric Gouaux |
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| Institution: | 1. Center for Neuroscience, Aging, and Stem Cell Research, Burnham Institute for Medical Research, La Jolla, CA, USA;2. These authors contributed equally to this work;3. Vollum Institute, Oregon Health and Science University, Portland, OR, USA;4. Department of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, New York, NY, USA;5. Howard Hughes Medical Institute, Oregon Health and Science University, Portland, OR, USA |
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| Abstract: | Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand‐gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular‐domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino‐terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily‐specific receptor assembly is not known. Here we show that AMPA receptor GluR1‐ and GluR2‐ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2‐ATD, propose mechanisms by which the ATD guides subfamily‐specific receptor assembly. |
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| Keywords: | amino‐terminal domain GluR2 glutamate receptor ion channel x‐ray crystallography |
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