9C60
CryoEM structure of kainate receptor Gluk2 in apo state
9C60 の概要
| エントリーDOI | 10.2210/pdb9c60/pdb |
| EMDBエントリー | 45239 |
| 分子名称 | Glutamate receptor ionotropic, kainate 2, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| 機能のキーワード | c1, membrane, homotetrmer, glutamate, structural 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 | 412990.62 |
| 構造登録者 | |
| 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 Cited by 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: 40442317DOI: 10.1038/s41594-025-01566-w 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.8 Å) |
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