1Y20

Crystal structure of the NR1 ligand-binding core in complex with ACPC

1Y20 の概要

• エントリーDOI: 10.2210/pdb1y20/pdb
• 関連するPDBエントリー: 1PB7 1PB8 1PB9 1PBQ 1Y1M 1Y1Z
• 分子名称: Glutamate [NMDA] receptor subunit zeta 1, 1-AMINOCYCLOPROPANECARBOXYLIC ACID (3 entities in total)
• 機能のキーワード: protein-ligand complex; ligand-binding complex, ligand binding protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : P35439
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33441.14

構造登録者

Inanobe, A.,Gouaux, E. (登録日: 2004-11-19, 公開日: 2005-07-12, 最終更新日: 2025-03-26)

主引用文献

Inanobe, A.,Furukawa, H.,Gouaux, E.
Mechanism of Partial Agonist Action at the NR1 Subunit of NMDA Receptors.
Neuron, 47:71-84, 2005

PubMed Abstract: Partial agonists produce submaximal activation of ligand-gated ion channels. To address the question of partial agonist action at the NR1 subunit of the NMDA receptor, we performed crystallographic and electrophysiological studies with 1-aminocyclopropane-1-carboxylic acid (ACPC), 1-aminocyclobutane-1-carboxylic acid (ACBC), and 1-aminocyclopentane-1-carboxylic acid (cycloleucine), three compounds with incrementally larger carbocyclic rings. Whereas ACPC and ACBC partially activate the NMDA receptor by 80% and 42%, respectively, their cocrystal structures of the NR1 ligand binding core show the same degree of domain closure as found in the complex with glycine, a full agonist, illustrating that the NR1 subunit provides a new paradigm for partial agonist action that is distinct from that of the evolutionarily related GluR2, AMPA-sensitive receptor. Cycloleucine behaves as an antagonist and stabilizes an open-cleft conformation. The NR1-cycloleucine complex forms a dimer that is similar to the GluR2 dimer, thereby suggesting a conserved mode of subunit-subunit interaction in AMPA and NMDA receptors.

PubMed: 15996549
DOI: 10.1016/j.neuron.2005.05.022

実験手法

X-RAY DIFFRACTION (1.4 Å)