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

Yan Zhao | Zendy; Shanshuang Chen | Zendy; Adam Swensen | Zendy; Weijun Qian | Zendy; Eric Gouaux | Zendy

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

Author(s) -

Yan Zhao,

Shanshuang Chen,

Adam Swensen,

Weijun Qian,

Eric Gouaux

Publication year - 2019

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aaw8250

Subject(s) - ampa receptor , protein subunit , receptor , ion channel , biophysics , glutamate receptor , chemistry , tetramer , population , ligand gated ion channel , biology , microbiology and biotechnology , neuroscience , biochemistry , gene , demography , sociology , enzyme

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. Zhaoet 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

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