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

Yan Zhao, Shanshuang Chen, Craig Yoshioka, Isabelle Baconguis and Eric Gouaux ()
Additional contact information
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

Nature, 2016, vol. 536, issue 7614, 108-111

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.

Date: 2016
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature18961 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:536:y:2016:i:7614:d:10.1038_nature18961

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature18961

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().