3BFU

Structure of the ligand-binding core of GluR2 in complex with the agonist (R)-TDPA at 1.95 A resolution

3BFU の概要

• エントリーDOI: 10.2210/pdb3bfu/pdb
• 関連するPDBエントリー: 1FTM 3BFT
• 分子名称: Glutamate receptor 2, (2R)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid (3 entities in total)
• 機能のキーワード: ampa receptor, glur2, ligand-binding core, agonist, (r)-tdpa, alternative splicing, cell junction, endoplasmic reticulum, glycoprotein, ion transport, ionic channel, lipoprotein, membrane, palmitate, phosphoprotein, postsynaptic cell membrane, rna editing, synapse, transmembrane, transport, 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: P19491
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 117643.50

構造登録者

Beich-Frandsen, M.,Mirza, O.,Vestergaard, B.,Gajhede, M.,Kastrup, J.S. (登録日: 2007-11-23, 公開日: 2008-10-14, 最終更新日: 2024-10-16)

主引用文献

Beich-Frandsen, M.,Pickering, D.S.,Mirza, O.,Johansen, T.N.,Greenwood, J.,Vestergaard, B.,Schousboe, A.,Gajhede, M.,Liljefors, T.,Kastrup, J.S.
Structures of the ligand-binding core of iGluR2 in complex with the agonists (R)- and (S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propionic acid explain their unusual equipotency.
J.Med.Chem., 51:1459-1463, 2008

PubMed Abstract: AMPA-type ionotropic glutamate receptors generally display high stereoselectivity in agonist binding. However, the stereoisomers of 2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propionic acid (TDPA) have similar enantiopharmacology. To understand this observation, we have determined the X-ray structures of ( R)-TDPA and ( S)-TDPA in complex with the ligand-binding core of iGluR2 and investigated the binding pharmacology at AMPA and kainate receptors. Both enantiomers induce full domain closure in iGluR2 but adopt different conformations when binding to the receptor, which may explain the similar enantiopharmacology.

PubMed: 18269227
DOI: 10.1021/jm701126w

実験手法

X-RAY DIFFRACTION (1.95 Å)