3JPW

Crystal structure of amino terminal domain of the NMDA receptor subunit NR2B

3JPW の概要

• エントリーDOI: 10.2210/pdb3jpw/pdb
• 関連するPDBエントリー: 3JPY
• 分子名称: Glutamate [NMDA] receptor subunit epsilon-2, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: nmda receptor, amino terminal domain, phenylethanolamine, cell junction, cell membrane, glycoprotein, ion transport, ionic channel, magnesium, membrane, phosphoprotein, postsynaptic cell membrane, receptor, synapse, transmembrane, transport, transport protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42348.93

構造登録者

Karakas, E.,Simorowski, N.,Furukawa, H. (登録日: 2009-09-04, 公開日: 2009-12-08, 最終更新日: 2024-10-30)

主引用文献

Karakas, E.,Simorowski, N.,Furukawa, H.
Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit.
Embo J., 28:3910-3920, 2009

PubMed Abstract: N-methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors (iGluRs) that mediate the majority of fast excitatory synaptic transmission in the mammalian brain. One of the hallmarks for the function of NMDA receptors is that their ion channel activity is allosterically regulated by binding of modulator compounds to the extracellular amino-terminal domain (ATD) distinct from the L-glutamate-binding domain. The molecular basis for the ATD-mediated allosteric regulation has been enigmatic because of a complete lack of structural information on NMDA receptor ATDs. Here, we report the crystal structures of ATD from the NR2B NMDA receptor subunit in the zinc-free and zinc-bound states. The structures reveal the overall clamshell-like architecture distinct from the non-NMDA receptor ATDs and molecular determinants for the zinc-binding site, ion-binding sites, and the architecture of the putative phenylethanolamine-binding site.

PubMed: 19910922
DOI: 10.1038/emboj.2009.338

実験手法

X-RAY DIFFRACTION (2.803 Å)