9C7C

Diheteromeric GluN1/GluN2A (delM653) in nanodisc complexed with glycine, glutamate, and GNE-4123, open conformation

これはPDB形式変換不可エントリーです。

9C7C の概要

• エントリーDOI: 10.2210/pdb9c7c/pdb
• EMDBエントリー: 45279
• 分子名称: Glutamate receptor ionotropic, NMDA 1,Green fluorescent protein, GLUTAMIC ACID, DECANE, ... (12 entities in total)
• 機能のキーワード: ion channel, nmda, positive allosteric modulator, open pore conformation, transport protein
• 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: 518213.05

構造登録者

Jalali-Yazdi, F.,Kim, J.,Gouaux, E. (登録日: 2024-06-10, 公開日: 2025-09-24, 最終更新日: 2026-02-04)

主引用文献

Abbott, J.A.,Kim, J.,Liu, B.,Popescu, G.K.,Gouaux, E.,Jalali-Yazdi, F.
Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements.
Sci Adv, 11:eadx4647-eadx4647, 2025

PubMed Abstract: Canonical -methyl-d-aspartate receptors (NMDARs) are glutamate-gated ion channels with critical roles in the development and function of the nervous system. The excitatory currents they produce reflect stochastic transitions between multiple agonist-bound closed- and open-pore states. We leveraged the intrinsically high open probability () of NMDARs composed of GluN1 and GluN2A subunits, together with judiciously chosen mutants and ligands, to achieve conditions in which receptors had a near unity. Using single-particle cryo-electron microscopy (cryo-EM), we captured three activated receptor states, each with distinct conformations of the gate-forming M3 helices. Separately, we carried out single-channel electrophysiology, together with statistical modeling, to relate the cryo-EM structures to the gating reaction. NMDAR channel opening involves bending of the pore-forming M3 helices to produce a transient open-channel conformation, subsequently stabilized by new interactions between the D2-M3 linkers with the pre-M1 helices and the pre-M4 loops, to yield the stable open channel.

PubMed: 40991709
DOI: 10.1126/sciadv.adx4647

実験手法

ELECTRON MICROSCOPY (3.1 Å)