1PB8

CRYSTAL STRUCTURE OF THE NR1 LIGAND BINDING CORE IN COMPLEX WITH D-SERINE AT 1.45 ANGSTROMS RESOLUTION

1PB8 の概要

• エントリーDOI: 10.2210/pdb1pb8/pdb
• 関連するPDBエントリー: 1PB7 1PB9
• 分子名称: N-methyl-D-aspartate Receptor Subunit 1, D-SERINE (3 entities in total)
• 機能のキーワード: ligand binding receptor; rat; nr1, 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: 33432.13

構造登録者

Furukawa, H.,Gouaux, E. (登録日: 2003-05-14, 公開日: 2003-06-24, 最終更新日: 2017-07-26)

主引用文献

Furukawa, H.,Gouaux, E.
Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core
Embo J., 22:2873-2885, 2003

PubMed Abstract: Excitatory neurotransmission mediated by the N-methyl-D-aspartate subtype of ionotropic glutamate receptors is fundamental to the development and function of the mammalian central nervous system. NMDA receptors require both glycine and glutamate for activation with NR1 and NR2 forming glycine and glutamate sites, respectively. Mechanisms to describe agonist and antagonist binding, and activation and desensitization of NMDA receptors have been hampered by the lack of high-resolution structures. Here, we describe the cocrystal structures of the NR1 S1S2 ligand-binding core with the agonists glycine and D-serine (DS), the partial agonist D-cycloserine (DCS) and the antagonist 5,7-dichlorokynurenic acid (DCKA). The cleft of the S1S2 'clamshell' is open in the presence of the antagonist DCKA and closed in the glycine, DS and DCS complexes. In addition, the NR1 S1S2 structure reveals the fold and interactions of loop 1, a cysteine-rich region implicated in intersubunit allostery.

PubMed: 12805203
DOI: 10.1093/emboj/cdg303

実験手法

X-RAY DIFFRACTION (1.45 Å)