2I0C

Crystal structure of the GluR6 ligand binding core dimer crosslinked by disulfide bonds between Y490C and L752C at 2.25 Angstroms Resolution

2I0C の概要

• エントリーDOI: 10.2210/pdb2i0c/pdb
• 関連するPDBエントリー: 1LB8 1YAE 2F36 2I0B
• 分子名称: Glutamate receptor, ionotropic kainate 2, GLUTAMIC ACID (3 entities in total)
• 機能のキーワード: 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 : P42260
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58813.36

構造登録者

Mayer, M.L. (登録日: 2006-08-10, 公開日: 2006-11-21, 最終更新日: 2024-11-20)

主引用文献

Weston, M.C.,Schuck, P.,Ghosal, A.,Rosenmund, C.,Mayer, M.L.
Conformational restriction blocks glutamate receptor desensitization.
Nat.Struct.Mol.Biol., 13:1120-1127, 2006

PubMed Abstract: Desensitization is a universal feature of ligand-gated ion channels. Using the crystal structure of the GluR2 L483Y mutant channel as a guide, we attempted to build non-desensitizing kainate-subtype glutamate receptors. Success was achieved for GluR5, GluR6 and GluR7 with intermolecular disulfide cross-links but not by engineering the dimer interface. Crystallographic analysis of the GluR6 Y490C L752C dimer revealed relaxation from the active conformation, which functional studies reveal is not sufficient to trigger desensitization. The equivalent non-desensitizing cross-linked GluR2 mutant retained weak sensitivity to a positive allosteric modulator, which had no effect on GluR2 L483Y. These results establish that the active conformation of AMPA and kainate receptors is conserved and further show that their desensitization requires dimer rearrangements, that subtle structural differences account for their diverse functional properties and that the ligand-binding core dimer is a powerful regulator of ion-channel activity.

PubMed: 17115050
DOI: 10.1038/nsmb1178

実験手法

X-RAY DIFFRACTION (2.25 Å)