1S50

X-ray structure of the GluR6 ligand binding core (S1S2A) in complex with glutamate at 1.65 A resolution

1S50 の概要

• エントリーDOI: 10.2210/pdb1s50/pdb
• 分子名称: Glutamate Receptor 6, 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: 1
• 化学式量合計: 29518.76

構造登録者

Mayer, M.L. (登録日: 2004-01-19, 公開日: 2005-02-08, 最終更新日: 2024-11-06)

主引用文献

Mayer, M.L.
Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity
Neuron, 45:539-552, 2005

PubMed Abstract: Little is known about the molecular mechanisms underlying differences in the ligand binding properties of AMPA, kainate, and NMDA subtype glutamate receptors. Crystal structures of the GluR5 and GluR6 kainate receptor ligand binding cores in complexes with glutamate, 2S,4R-4-methylglutamate, kainate, and quisqualate have now been solved. The structures reveal that the ligand binding cavities are 40% (GluR5) and 16% (GluR6) larger than for GluR2. The binding of AMPA- and GluR5-selective agonists to GluR6 is prevented by steric occlusion, which also interferes with the high-affinity binding of 2S,4R-4-methylglutamate to AMPA receptors. Strikingly, the extent of domain closure produced by the GluR6 partial agonist kainate is only 3 degrees less than for glutamate and 11 degrees greater than for the GluR2 kainate complex. This, together with extensive interdomain contacts between domains 1 and 2 of GluR5 and GluR6, absent from AMPA receptors, likely contributes to the high stability of GluR5 and GluR6 kainate complexes.

PubMed: 15721240
DOI: 10.1016/j.neuron.2005.01.031

実験手法

X-RAY DIFFRACTION (1.65 Å)