2A5S

Crystal Structure Of The NR2A Ligand Binding Core In Complex With Glutamate

2A5S の概要

• エントリーDOI: 10.2210/pdb2a5s/pdb
• 関連するPDBエントリー: 1PB7 2A5T
• 分子名称: N-methyl-D-aspartate receptor NMDAR2A subunit, GLUTAMIC ACID (3 entities in total)
• 機能のキーワード: protein-ligand complex, metal transport, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31999.52

構造登録者

Furukawa, H.,Singh, S.K.,Mancusso, R.,Gouaux, E. (登録日: 2005-06-30, 公開日: 2005-11-15, 最終更新日: 2024-10-30)

主引用文献

Furukawa, H.,Singh, S.K.,Mancusso, R.,Gouaux, E.
Subunit arrangement and function in NMDA receptors
Nature, 438:185-192, 2005

PubMed 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.

PubMed: 16281028
DOI: 10.1038/nature04089

実験手法

X-RAY DIFFRACTION (1.7 Å)