5FTI

Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (lithium form)

5FTI の概要

• エントリーDOI: 10.2210/pdb5fti/pdb
• 関連するPDBエントリー: 5FTH
• 分子名称: GLUTAMATE RECEPTOR 2, GLUTAMIC ACID, LITHIUM ION, ... (6 entities in total)
• 機能のキーワード: signaling protein
• 由来する生物種: RATTUS NORVEGICUS (NORWAY RAT)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P19491
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65404.76

構造登録者

Nayeem, N.,Green, T. (登録日: 2016-01-13, 公開日: 2016-02-03, 最終更新日: 2024-11-20)

主引用文献

Dawe, G.B.,Musgaard, M.,Aurousseau, M.R.P.,Nayeem, N.,Green, T.,Biggin, P.C.,Bowie, D.
Distinct Structural Pathways Coordinate the Activation of Ampa Receptor-Auxiliary Subunit Complexes.
Neuron, 89:1264-, 2016

PubMed Abstract: Neurotransmitter-gated ion channels adopt different gating modes to fine-tune signaling at central synapses. At glutamatergic synapses, high and low activity of AMPA receptors (AMPARs) is observed when pore-forming subunits coassemble with or without auxiliary subunits, respectively. Whether a common structural pathway accounts for these different gating modes is unclear. Here, we identify two structural motifs that determine the time course of AMPAR channel activation. A network of electrostatic interactions at the apex of the AMPAR ligand-binding domain (LBD) is essential for gating by pore-forming subunits, whereas a conserved motif on the lower, D2 lobe of the LBD prolongs channel activity when auxiliary subunits are present. Accordingly, channel activity is almost entirely abolished by elimination of the electrostatic network but restored via auxiliary protein interactions at the D2 lobe. In summary, we propose that activation of native AMPAR complexes is coordinated by distinct structural pathways, favored by the association/dissociation of auxiliary subunits.

PubMed: 26924438
DOI: 10.1016/J.NEURON.2016.01.038

実験手法

X-RAY DIFFRACTION (1.35 Å)