Published in

American Association for the Advancement of Science, Science, 6438(364), p. 355-362, 2019

DOI: 10.1126/science.aaw8250

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

This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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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