3C31

Crystal structure of GluR5 ligand-binding core in complex with lithium at 1.49 Angstrom resolution

3C31 の概要

• エントリーDOI: 10.2210/pdb3c31/pdb
• 関連するPDBエントリー: 1TT1 2F34 2OJT 2PBW 3C32 3C33 3C34 3C35 3C36
• 分子名称: GLUTAMATE RECEPTOR, IONOTROPIC KAINATE 1, LITHIUM ION, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P22756
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59553.72

構造登録者

Mayer, M.L. (登録日: 2008-01-27, 公開日: 2008-06-17, 最終更新日: 2023-08-30)

主引用文献

Plested, A.J.,Vijayan, R.,Biggin, P.C.,Mayer, M.L.
Molecular basis of kainate receptor modulation by sodium.
Neuron, 58:720-735, 2008

PubMed Abstract: Membrane proteins function in a polarized ionic environment with sodium-rich extracellular and potassium-rich intracellular solutions. Glutamate receptors that mediate excitatory synaptic transmission in the brain show unusual sensitivity to external ions, resulting in an apparent requirement for sodium in order for glutamate to activate kainate receptors. Here, we solve the structure of the Na(+)-binding sites and determine the mechanism by which allosteric anions and cations regulate ligand-binding dimer stability, and hence the rate of desensitization and receptor availability for gating by glutamate. We establish a stoichiometry for binding of 2 Na(+) to 1 Cl(-) and show that allosteric anions and cations bind at physically discrete sites with strong electric fields, that the binding sites are not saturated in CSF, and that the requirement of kainate receptors for Na(+) occurs simply because other cations bind with lower affinity and have lower efficacy compared to Na(+).

PubMed: 18549784
DOI: 10.1016/j.neuron.2008.04.001

実験手法

X-RAY DIFFRACTION (1.49 Å)