7F5B

LBD-TMD focused reconstruction of DNQX-bound GluK2-1xNeto2 complex

7F5B の概要

• エントリーDOI: 10.2210/pdb7f5b/pdb
• EMDBエントリー: 31464
• 分子名称: Glutamate receptor ionotropic, kainate 2, Neuropilin and tolloid-like protein 2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: ionotropic glutamate receptors, single-pass transmembrane proteins, membrane protein
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 472608.93

構造登録者

He, L.L.,Gao, Y.W.,Li, B.,Zhao, Y. (登録日: 2021-06-21, 公開日: 2021-09-29, 最終更新日: 2025-07-02)

主引用文献

He, L.,Sun, J.,Gao, Y.,Li, B.,Wang, Y.,Dong, Y.,An, W.,Li, H.,Yang, B.,Ge, Y.,Zhang, X.C.,Shi, Y.S.,Zhao, Y.
Kainate receptor modulation by NETO2.
Nature, 599:325-329, 2021

PubMed Abstract: Glutamate-gated kainate receptors are ubiquitous in the central nervous system of vertebrates, mediate synaptic transmission at the postsynapse and modulate transmitter release at the presynapse. In the brain, the trafficking, gating kinetics and pharmacology of kainate receptors are tightly regulated by neuropilin and tolloid-like (NETO) proteins. Here we report cryo-electron microscopy structures of homotetrameric GluK2 in complex with NETO2 at inhibited and desensitized states, illustrating variable stoichiometry of GluK2-NETO2 complexes, with one or two NETO2 subunits associating with GluK2. We find that NETO2 accesses only two broad faces of kainate receptors, intermolecularly crosslinking the lower lobe of ATD, the upper lobe of LBD and the lower lobe of LBD, illustrating how NETO2 regulates receptor-gating kinetics. The transmembrane helix of NETO2 is positioned proximal to the selectivity filter and competes with the amphiphilic H1 helix after M4 for interaction with an intracellular cap domain formed by the M1-M2 linkers of the receptor, revealing how rectification is regulated by NETO2.

PubMed: 34552241
DOI: 10.1038/s41586-021-03936-y

実験手法

ELECTRON MICROSCOPY (3.9 Å)