Subunit arrangement and function in NMDA receptors

Hiroyasu Furukawa, Satinder K Singh, Romina Mancusso and Eric Gouaux ()
Additional contact information
Hiroyasu Furukawa: Department of Biochemistry and Molecular Biophysics
Satinder K Singh: Department of Biochemistry and Molecular Biophysics
Romina Mancusso: Department of Biochemistry and Molecular Biophysics
Eric Gouaux: Department of Biochemistry and Molecular Biophysics

Nature, 2005, vol. 438, issue 7065, 185-192

Abstract: Abstract Excitatory neurotransmission mediated by NMDA (N-methyl-d-aspartate) receptors is fundamental to the physiology of the mammalian central nervous system. These receptors are heteromeric ion channels that for activation require binding of glycine and glutamate to the NR1 and NR2 subunits, respectively. NMDA receptor function is characterized by slow channel opening and deactivation, and the resulting influx of cations initiates signal transduction cascades that are crucial to higher functions including learning and memory. Here we report crystal structures of the ligand-binding core of NR2A with glutamate and that of the NR1–NR2A heterodimer with glutamate and glycine. The NR2A–glutamate complex defines the determinants of glutamate and NMDA recognition, and the NR1–NR2A heterodimer suggests a mechanism for ligand-induced ion channel opening. Analysis of the heterodimer interface, together with biochemical and electrophysiological experiments, confirms that the NR1–NR2A heterodimer is the functional unit in tetrameric NMDA receptors and that tyrosine 535 of NR1, located in the subunit interface, modulates the rate of ion channel deactivation.

Date: 2005
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature04089 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:438:y:2005:i:7065:d:10.1038_nature04089

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

DOI: 10.1038/nature04089

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 ().