6UD3

Full length Glycine receptor reconstituted in lipid nanodisc in Gly/PTX-bound open/blocked conformation

6UD3 の概要

• エントリーDOI: 10.2210/pdb6ud3/pdb
• EMDBエントリー: 20731
• 分子名称: Glycine receptor subunit alphaZ1, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCINE, ... (4 entities in total)
• 機能のキーワード: ions ligands receptors, glycine receptor recombinant proteins glycine, membrane protein
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 264746.90

構造登録者

Kumar, A.,Basak, S.,Chakrapani, S. (登録日: 2019-09-18, 公開日: 2020-07-29, 最終更新日: 2024-03-20)

主引用文献

Kumar, A.,Basak, S.,Rao, S.,Gicheru, Y.,Mayer, M.L.,Sansom, M.S.P.,Chakrapani, S.
Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs.
Nat Commun, 11:3752-3752, 2020

PubMed Abstract: Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Glycine receptors (GlyRs) are key players in mediating fast inhibitory neurotransmission at these synapses. While previous high-resolution structures have provided insights into the molecular architecture of GlyR, several mechanistic questions pertaining to channel function are still unanswered. Here, we present Cryo-EM structures of the full-length GlyR protein complex reconstituted into lipid nanodiscs that are captured in the unliganded (closed), glycine-bound (open and desensitized), and allosteric modulator-bound conformations. A comparison of these states reveals global conformational changes underlying GlyR channel gating and modulation. The functional state assignments were validated by molecular dynamics simulations, and the observed permeation events are in agreement with the anion selectivity and conductance of GlyR. These studies provide the structural basis for gating, ion selectivity, and single-channel conductance properties of GlyR in a lipid environment.

PubMed: 32719334
DOI: 10.1038/s41467-020-17364-5

実験手法

ELECTRON MICROSCOPY (3.5 Å)