8BLJ

Crystal structure of the ligand-binding domain (LBD) of human iGluR Delta-1 (GluD1), apo state

8BLJ の概要

• エントリーDOI: 10.2210/pdb8blj/pdb
• 分子名称: Glutamate receptor ionotropic, delta-1,Isoform 2 of Glutamate receptor ionotropic, delta-1, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: ion channel, ligand binding domain, glutamate receptor, apo state, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 190091.96

構造登録者

Heroven, C.,Malinauskas, T.,Aricescu, A.R. (登録日: 2022-11-09, 公開日: 2023-11-22, 最終更新日: 2024-10-16)

主引用文献

Piot, L.,Heroven, C.,Bossi, S.,Zamith, J.,Malinauskas, T.,Johnson, C.,Wennagel, D.,Stroebel, D.,Charrier, C.,Aricescu, A.R.,Mony, L.,Paoletti, P.
GluD1 binds GABA and controls inhibitory plasticity.
Science, 382:1389-1394, 2023

PubMed Abstract: Fast synaptic neurotransmission in the vertebrate central nervous system relies primarily on ionotropic glutamate receptors (iGluRs), which drive neuronal excitation, and type A γ-aminobutyric acid receptors (GABARs), which are responsible for neuronal inhibition. However, the GluD1 receptor, an iGluR family member, is present at both excitatory and inhibitory synapses. Whether and how GluD1 activation may affect inhibitory neurotransmission is unknown. In this work, by using a combination of biochemical, structural, and functional analyses, we demonstrate that GluD1 binds GABA, a previously unknown feature of iGluRs. GluD1 activation produces long-lasting enhancement of GABAergic synaptic currents in the adult mouse hippocampus through a non-ionotropic mechanism that is dependent on trans-synaptic anchoring. The identification of GluD1 as a GABA receptor that controls inhibitory synaptic plasticity challenges the classical dichotomy between glutamatergic and GABAergic receptors.

PubMed: 38060673
DOI: 10.1126/science.adf3406

実験手法

X-RAY DIFFRACTION (2.18 Å)