4IO2

Crystal Structure of the AvGluR1 ligand binding domain complex with glutamate at 1.37 Angstrom resolution

4IO2 の概要

• エントリーDOI: 10.2210/pdb4io2/pdb
• 関連するPDBエントリー: 4IO3 4IO4 4IO5 4IO6 4IO7 4IO8
• 分子名称: Glutamate receptor 1, CHLORIDE ION, GLUTAMIC ACID, ... (4 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Adineta vaga (Rotifer); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55420.98

構造登録者

Lomash, S.,Chittori, S.,Mayer, M.L. (登録日: 2013-01-07, 公開日: 2013-02-20, 最終更新日: 2024-11-27)

主引用文献

Lomash, S.,Chittori, S.,Brown, P.,Mayer, M.L.
Anions Mediate Ligand Binding in Adineta vaga Glutamate Receptor Ion Channels.
Structure, 21:414-425, 2013

PubMed Abstract: AvGluR1, a glutamate receptor ion channel from the primitive eukaryote Adineta vaga, is activated by alanine, cysteine, methionine, and phenylalanine, which produce lectin-sensitive desensitizing responses like those to glutamate, aspartate, and serine. AvGluR1 LBD crystal structures reveal an unusual scheme for binding dissimilar ligands that may be utilized by distantly related odorant/chemosensory receptors. Arginine residues in domain 2 coordinate the γ-carboxyl group of glutamate, whereas in the alanine, methionine, and serine complexes a chloride ion acts as a surrogate ligand, replacing the γ-carboxyl group. Removal of Cl(-) lowers affinity for these ligands but not for glutamate or aspartate nor for phenylalanine, which occludes the anion binding site and binds with low affinity. AvGluR1 LBD crystal structures and sedimentation analysis also provide insights into the evolutionary link between prokaryotic and eukaryotic iGluRs and reveal features unique to both classes, emphasizing the need for additional structure-based studies on iGluR-ligand interactions.

PubMed: 23434404
DOI: 10.1016/j.str.2013.01.006

実験手法

X-RAY DIFFRACTION (1.37 Å)