3G3F

Crystal structure of the GluR6 ligand binding domain dimer with glutamate and NaCl at 1.38 Angstrom resolution

3G3F の概要

• エントリーDOI: 10.2210/pdb3g3f/pdb
• 関連するPDBエントリー: 3G3G 3G3H 3G3I 3G3J 3G3K
• 分子名称: Glutamate receptor, ionotropic kainate 2, GLUTAMIC ACID, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: membrane protein, cell junction, cell membrane, glycoprotein, ion transport, ionic channel, membrane, postsynaptic cell membrane, receptor, rna editing, synapse, transmembrane, transport
• 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 : P42260
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59285.13

構造登録者

Chaudhry, C.,Mayer, M.L. (登録日: 2009-02-02, 公開日: 2009-06-02, 最終更新日: 2024-10-30)

主引用文献

Chaudhry, C.,Weston, M.C.,Schuck, P.,Rosenmund, C.,Mayer, M.L.
Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.
Embo J., 28:1518-1530, 2009

PubMed Abstract: AMPA and kainate receptors mediate fast synaptic transmission. AMPA receptor ligand-binding domains form dimers, which are key functional units controlling ion-channel activation and desensitization. Dimer stability is inversely related to the rate and extent of desensitization. Kainate and AMPA receptors share common structural elements, but functional measurements suggest that subunit assembly and gating differs between these subtypes. To investigate this, we constructed a library of GluR6 kainate receptor mutants and directly measured changes in kainate receptor dimer stability by analytical ultracentrifugation, which, combined with electrophysiological experiments, revealed an inverse correlation between dimer stability and the rate of desensitization. We solved crystal structures for a series of five GluR6 mutants, to understand the molecular mechanisms for dimer stabilization. We demonstrate that the desensitized state of kainate receptors acts as a deep energy well offsetting the stabilizing effects of dimer interface mutants, and that the deactivation of kainate receptor responses is dominated by entry into desensitized states. Our results show how neurotransmitter receptors with similar structures and gating mechanisms can exhibit strikingly different functional properties.

PubMed: 19339989
DOI: 10.1038/emboj.2009.86

実験手法

X-RAY DIFFRACTION (1.377 Å)