8GC5

Domoate-bound GluK2 kainate receptors in non-active conformation

8GC5 の概要

• エントリーDOI: 10.2210/pdb8gc5/pdb
• EMDBエントリー: 29929
• 分子名称: Glutamate receptor ionotropic, kainate 2, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: ion channel, glutamate kainate receptor 2, homotetramer, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 404438.20

構造登録者

Bogdanovic, N.,Tajima, N. (登録日: 2023-03-01, 公開日: 2024-03-13, 最終更新日: 2025-09-24)

主引用文献

Segura-Covarrubias, G.,Zhou, C.,Bogdanovic, N.,Zhang, L.,Tajima, N.
Structural basis of GluK2 kainate receptor activation by a partial agonist.
Nat.Struct.Mol.Biol., 32:1456-1469, 2025

PubMed Abstract: Kainate receptors (KARs) belong to the family of ionotropic glutamate receptors that regulate neurotransmitter release and excitatory synaptic transmission in the central nervous system. Despite their critical roles in synaptic signaling and disease, the detailed gating mechanisms of KARs are not completely understood. Here we present cryo-electron microscopy structures of homomeric rat GluK2 KAR in an unliganded apo state and in complexes with a partial agonist, domoate. Partial agonist-bound GluK2 populates multiple conformations, including intermediate and desensitized states. Moreover, we demonstrate that the N-glycans at the amino-terminal domain-ligand binding domain (LBD) interface modulate receptor gating properties by interfering with cation binding at the LBD dimer interface. Together, these results provide insights into the unique gating mechanisms of KARs.

PubMed: 40442317
DOI: 10.1038/s41594-025-01566-w

実験手法

ELECTRON MICROSCOPY (3.93 Å)