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Architecture of fully occupied GluA2 AMPA receptor–TARP complex elucidated by cryo-EM

Author

Listed:
  • Yan Zhao

    (Vollum Institute, Oregon Health & Science University)

  • Shanshuang Chen

    (Vollum Institute, Oregon Health & Science University)

  • Craig Yoshioka

    (Oregon Health & Science University)

  • Isabelle Baconguis

    (Vollum Institute, Oregon Health & Science University)

  • Eric Gouaux

    (Vollum Institute, Oregon Health & Science University
    Howard Hughes Medical Institute, Oregon Health & Science University)

Abstract

The cryo-electron microscopy structure of the homomeric GluA2 AMPA receptor in the presence of TARP γ2 subunits is reported, which reveals that TARPs are arranged around the ion channel domain and underneath the ligand-binding domains, poised to modulate receptor activity.

Suggested Citation

  • Yan Zhao & Shanshuang Chen & Craig Yoshioka & Isabelle Baconguis & Eric Gouaux, 2016. "Architecture of fully occupied GluA2 AMPA receptor–TARP complex elucidated by cryo-EM," Nature, Nature, vol. 536(7614), pages 108-111, August.
    • Handle: RePEc:nat:nature:v:536:y:2016:i:7614:d:10.1038_nature18961
    DOI: 10.1038/nature18961
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    Cited by:

    1. Amanda M. Perozzo & Jochen Schwenk & Aichurok Kamalova & Terunaga Nakagawa & Bernd Fakler & Derek Bowie, 2023. "GSG1L-containing AMPA receptor complexes are defined by their spatiotemporal expression, native interactome and allosteric sites," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Diogo Bessa-Neto & Gerti Beliu & Alexander Kuhlemann & Valeria Pecoraro & Sören Doose & Natacha Retailleau & Nicolas Chevrier & David Perrais & Markus Sauer & Daniel Choquet, 2021. "Bioorthogonal labeling of transmembrane proteins with non-canonical amino acids unveils masked epitopes in live neurons," Nature Communications, Nature, vol. 12(1), pages 1-16, December.

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