3DP6

Crystal structure of the binding domain of the AMPA subunit GluR2 bound to glutamate

3DP6 の概要

• エントリーDOI: 10.2210/pdb3dp6/pdb
• 関連するPDBエントリー: 3DLN 3DP4
• 分子名称: Glutamate receptor 2, ZINC ION, GLUTAMIC ACID, ... (4 entities in total)
• 機能のキーワード: glutamate receptor, glur2, ampa receptor, neurotransmitter receptor, s1s2, alternative splicing, cell junction, endoplasmic reticulum, glycoprotein, ion transport, ionic channel, lipoprotein, membrane, palmitate, phosphoprotein, postsynaptic cell membrane, rna editing, synapse, transmembrane, transport, signaling protein
• 由来する生物種: Rattus norvegicus; 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: 3
• 化学式量合計: 93265.16

構造登録者

Ahmed, A.H.,Wang, Q.,Sondermann, H.,Oswald, R.E. (登録日: 2008-07-07, 公開日: 2008-11-25, 最終更新日: 2024-10-30)

主引用文献

Ahmed, A.H.,Wang, Q.,Sondermann, H.,Oswald, R.E.
Structure of the S1S2 glutamate binding domain of GLuR3.
Proteins, 75:628-637, 2008

PubMed Abstract: Glutamate receptors are the most prevalent excitatory neurotransmitter receptors in the vertebrate central nervous system. Determining the structural differences between the binding sites of different subtypes is crucial to our understanding of neuronal circuits and to the development of subtype specific drugs. The structures of the binding domain (S1S2) of the GluR3 (flip) AMPA receptor subunit bound to glutamate and AMPA and the GluR2 (flop) subunit bound to glutamate were determined by X-ray crystallography to 1.9, 2.1, and 1.55 A, respectively. Overall, the structure of GluR3 (flip) S1S2 is very similar to GluR2 (flop) S1S2 (backbone RMSD of 0.30 +/- 0.05 for glutamate-bound and 0.26 +/- 0.01 for AMPA-bound). The differences in the flip and flop isoforms are subtle and largely arise from one hydrogen bond across the dimer interface and associated water molecules. Comparison of the binding affinity for various agonists and partial agonists suggest that the S1S2 domains of GluR2 and GluR3 show only small differences in affinity, unlike what is found for the intact receptors (with the exception of one ligand, Cl-HIBO, which has a 10-fold difference in affinity for GluR2 vs. GluR3).

PubMed: 19003990
DOI: 10.1002/prot.22274

実験手法

X-RAY DIFFRACTION (1.55 Å)