4KCD

Crystal Structure of the NMDA Receptor GluN3A Ligand Binding Domain Apo State

4KCD の概要

• エントリーDOI: 10.2210/pdb4kcd/pdb
• 関連するPDBエントリー: 2RC7 2RC8 2RC9 4KCC
• 分子名称: Glutamate receptor ionotropic, NMDA 3A, GLYCEROL (3 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: Q9R1M7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66056.79

構造登録者

Yao, Y.,Lau, A.Y.,Mayer, M.L. (登録日: 2013-04-24, 公開日: 2013-07-31, 最終更新日: 2024-10-16)

主引用文献

Yao, Y.,Belcher, J.,Berger, A.J.,Mayer, M.L.,Lau, A.Y.
Conformational Analysis of NMDA Receptor GluN1, GluN2, and GluN3 Ligand-Binding Domains Reveals Subtype-Specific Characteristics.
Structure, 21:1788-1799, 2013

PubMed Abstract: The NMDA receptor family of glutamate receptor ion channels is formed by obligate heteromeric assemblies of GluN1, GluN2, and GluN3 subunits. GluN1 and GluN3 bind glycine, whereas GluN2 binds glutamate. Crystal structures of the GluN1 and GluN3A ligand-binding domains (LBDs) in their apo states unexpectedly reveal open- and closed-cleft conformations, respectively, with water molecules filling the binding pockets. Computed conformational free energy landscapes for GluN1, GluN2A, and GluN3A LBDs reveal that the apo-state LBDs sample closed-cleft conformations, suggesting that their agonists bind via a conformational selection mechanism. By contrast, free energy landscapes for the AMPA receptor GluA2 LBD suggest binding of glutamate via an induced-fit mechanism. Principal component analysis reveals a rich spectrum of hinge bending, rocking, twisting, and sweeping motions that are different for the GluN1, GluN2A, GluN3A, and GluA2 LBDs. This variation highlights the structural complexity of signaling by glutamate receptor ion channels.

PubMed: 23972471
DOI: 10.1016/j.str.2013.07.011

実験手法

X-RAY DIFFRACTION (1.68 Å)