3OEM

Crystal structure of GluN2D ligand-binding core in complex with N-methyl-D-aspartate

3OEM の概要

• エントリーDOI: 10.2210/pdb3oem/pdb
• 関連するPDBエントリー: 3OEK 3OEL 3OEN
• 分子名称: Glutamate [NMDA] receptor subunit epsilon-4, N-methyl-D-aspartic acid (3 entities in total)
• 機能のキーワード: ion channel, n-methyl-d-aspartate, transport protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: Q62645
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32188.75

構造登録者

Simorowski, N.,Furukawa, H. (登録日: 2010-08-12, 公開日: 2011-05-11, 最終更新日: 2025-03-26)

主引用文献

Vance, K.M.,Simorowski, N.,Traynelis, S.F.,Furukawa, H.
Ligand-specific deactivation time course of GluN1/GluN2D NMDA receptors.
Nat Commun, 2:294-294, 2011

PubMed Abstract: N-methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors that mediate a majority of excitatory synaptic transmission. One unique property of GluN1/GluN2D NMDA receptors is an unusually prolonged deactivation time course following the removal of L-glutamate. Here we show, using x-ray crystallography and electrophysiology, that the deactivation time course of GluN1/GluN2D receptors is influenced by the conformational variability of the ligand-binding domain (LBD) as well as the structure of the activating ligand. L-glutamate and L-CCG-IV induce significantly slower deactivation time courses compared with other agonists. Crystal structures of the isolated GluN2D LBD in complex with various ligands reveal that the binding of L-glutamate induces a unique conformation at the backside of the ligand-binding site in proximity to the region at which the transmembrane domain would be located in the intact receptors. These data suggest that the activity of the GluN1/GluN2D NMDA receptor is controlled distinctively by the endogenous neurotransmitter L-glutamate.

PubMed: 21522138
DOI: 10.1038/ncomms1295

実験手法

X-RAY DIFFRACTION (1.9 Å)