2I3V

Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant

2I3V の概要

• エントリーDOI: 10.2210/pdb2i3v/pdb
• 関連するPDBエントリー: 1FTJ 2I3W
• 分子名称: Glutamate receptor 2, ZINC ION, GLUTAMIC ACID, ... (4 entities in total)
• 機能のキーワード: ionotropic glutamate receptor ligand binding core s1s2 g725c mutant, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P19491
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 117028.44

構造登録者

Armstrong, N.,Jasti, J.,Beich-Frandsen, M.,Gouaux, E. (登録日: 2006-08-21, 公開日: 2006-10-17, 最終更新日: 2024-10-30)

主引用文献

Armstrong, N.,Jasti, J.,Beich-Frandsen, M.,Gouaux, E.
Measurement of Conformational Changes accompanying Desensitization in an Ionotropic Glutamate Receptor.
Cell(Cambridge,Mass.), 127:85-97, 2006

PubMed Abstract: The canonical conformational states occupied by most ligand-gated ion channels, and many cell-surface receptors, are the resting, activated, and desensitized states. While the resting and activated states of multiple receptors are well characterized, elaboration of the structural properties of the desensitized state, a state that is by definition inactive, has proven difficult. Here we use electrical, chemical, and crystallographic experiments on the AMPA-sensitive GluR2 receptor, defining the conformational rearrangements of the agonist binding cores that occur upon desensitization of this ligand-gated ion channel. These studies demonstrate that desensitization involves the rupture of an extensive interface between domain 1 of 2-fold related glutamate-binding core subunits, compensating for the ca. 21 degrees of domain closure induced by glutamate binding. The rupture of the domain 1 interface allows the ion channel to close and thereby provides a simple explanation to the long-standing question of how agonist binding is decoupled from ion channel gating upon receptor desensitization.

PubMed: 17018279
DOI: 10.1016/j.cell.2006.08.037

実験手法

X-RAY DIFFRACTION (2.4 Å)