{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T18:23:10Z","timestamp":1791051790804,"version":"4.1.0"},"reference-count":50,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,9,1]]},"abstract":"<jats:p>The AMPA (\u03b1-amino-3-hydroxy-5-methylisoxazole-4-propionic acid) subfamily of iGluRs (ionotropic glutamate receptors) is essential for fast excitatory neurotransmission in the central nervous system. The malfunction of AMPARs (AMPA receptors) has been implicated in many neurological diseases, including Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis. The active channels of AMPARs and other iGluR subfamilies are tetramers formed exclusively by assembly of subunits within the same subfamily. It has been proposed that the assembly process is controlled mainly by the extracellular ATD (N-terminal domain) of iGluR. In addition, ATD has also been implicated in synaptogenesis, iGluR trafficking and trans-synaptic signalling, through unknown mechanisms. We report in the present study a 2.5\u00a0\u00c5 (1\u00a0\u00c5=0.1\u00a0nm) resolution crystal structure of the ATD of GluA1. Comparative analyses of the structure of GluA1-ATD and other subunits sheds light on our understanding of how ATD drives subfamily-specific assembly of AMPARs. In addition, analysis of the crystal lattice of GluA1-ATD suggests a novel mechanism by which the ATD might participate in inter-tetramer AMPAR clustering, as well as in trans-synaptic protein\u2013protein interactions.<\/jats:p>","DOI":"10.1042\/bj20110801","type":"journal-article","created":{"date-parts":[[2011,7,4]],"date-time":"2011-07-04T15:54:55Z","timestamp":1309794895000},"page":"255-263","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Crystal structure of the glutamate receptor GluA1 N-terminal domain"],"prefix":"10.1042","volume":"438","author":[{"given":"Guorui","family":"Yao","sequence":"first","affiliation":[{"name":"Fujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, College of Medicine, Xiamen University, Xiamen, Fujian 361005, China"},{"name":"Center for Neuroscience, Aging and Stem Cell Research, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yinong","family":"Zong","sequence":"additional","affiliation":[{"name":"Center for Neuroscience, Aging and Stem Cell Research, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shenyan","family":"Gu","sequence":"additional","affiliation":[{"name":"Center for Neuroscience, Aging and Stem Cell Research, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jie","family":"Zhou","sequence":"additional","affiliation":[{"name":"Center for Neuroscience, Aging and Stem Cell Research, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huaxi","family":"Xu","sequence":"additional","affiliation":[{"name":"Fujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, College of Medicine, Xiamen University, Xiamen, Fujian 361005, China"},{"name":"Center for Neuroscience, Aging and Stem Cell Research, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irimpan\u00a0I.","family":"Mathews","sequence":"additional","affiliation":[{"name":"Stanford Synchrotron Radiation Lightsource, 2575 Sand Hill Road, Menlo Park, CA 94025, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rongsheng","family":"Jin","sequence":"additional","affiliation":[{"name":"Center for Neuroscience, Aging and Stem Cell Research, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2011,8,12]]},"reference":[{"key":"2021112214520028100_B1","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/S0031-6997(24)01394-2","article-title":"The glutamate receptor ion channels","volume":"51","author":"Dingledine","year":"1999","journal-title":"Pharmacol. 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