9OBS

glutamate/glycine-bound GluN1a/2B NMDAR

9OBS の概要

• エントリーDOI: 10.2210/pdb9obs/pdb
• EMDBエントリー: 70297
• 分子名称: Glutamate receptor ionotropic, NMDA 1, Glutamate receptor ionotropic, NMDA 2B, GLYCINE, ... (5 entities in total)
• 機能のキーワード: membrane protein, ion channels, nmdar
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 384280.77

構造登録者

Steigerwald, R.,Furukawa, H. (登録日: 2025-04-23, 公開日: 2026-05-06, 最終更新日: 2026-06-24)

主引用文献

Steigerwald, R.,Epstein, M.,Chou, T.H.,Simorowski, N.,Furukawa, H.
Molecular mechanism of calcium permeability and magnesium block in NMDA receptors.
Nat.Neurosci., 29:1293-1302, 2026

PubMed Abstract: Hebbian neuroplasticity, which is thought to be a cellular substrate of learning and memory, can occur by means of coincidental detection of presynaptic neurotransmitter release and Ca influx upon postsynaptic depolarization. This is mediated at a molecular level by N-methyl-D-aspartate-type glutamate receptors, which bind glutamate and glycine and facilitate Ca influx upon relief of Mg channel block during membrane depolarization. However, the structural mechanism underlying Ca permeability and Mg blockade in N-methyl-D-aspartate-type glutamate receptors has yet to be fully elucidated. Here we demonstrate using single-particle cryo-electron microscopy that Ca permeation through the narrow constriction of the cation selectivity filter involves partial dehydration, as evidenced by several Ca binding sites. In contrast, Mg binds outside of the selectivity filter through a water network and remains hydrated, thereby acting as a channel blocker. Furthermore, the lipid network around the selectivity filter influences the stability of Mg binding in a voltage-dependent manner. Our study details the transmembrane chemistry essential for initiating neuroplasticity.

PubMed: 42086762
DOI: 10.1038/s41593-026-02283-3

実験手法

ELECTRON MICROSCOPY (3.18 Å)