Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM

Author:

Zhao Yan1ORCID,Chen Shanshuang1ORCID,Swensen Adam C.2ORCID,Qian Wei-Jun2ORCID,Gouaux Eric13ORCID

Affiliation:

1. Vollum Institute, Oregon Health and Science University, 3181 SW Sam Jackson Park Road, Portland, OR 97239, USA.

2. Integrative Omics, Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.

3. Howard Hughes Medical Institute, Oregon Health and Science University, 3181 SW Sam Jackson Park Road, Portland, OR 97239, USA.

Abstract

Diversity in ion channel complexes AMPA receptors are glutamate activated ion channels that mediate fast synaptic transmission in the nervous system and play a key role in learning and memory. The receptors are tetramers built from various combinations of four subunits, with functional diversity coming from the range of subunit compositions. Zhao et al. purified native receptors from rat brains and determined the structures of 10 different complexes by cryo–electron microscopy. Certain arrangements of the four subunits are preferred. The structure of a key gating element—a linker between the transmembrane and ligand binding domains—reveals how this receptor may function. Science , this issue p. 355

Funder

Howard Hughes Medical Institute

National Institute of General Medical Sciences

National Institute of Neurological Disorders and Stroke

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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