9NX0

Alpha7-nicotinic acetylcholine receptor bound to conotoxin ImI

9NX0 の概要

• エントリーDOI: 10.2210/pdb9nx0/pdb
• EMDBエントリー: 49897
• 分子名称: Alpha-conotoxin ImI, Neuronal acetylcholine receptor subunit alpha-7, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: ion channel, toxin, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 286535.31

構造登録者

Stowell, M.H.B.,Hibbs, R.E.,Noviello, C.M.,Bhattacharjee, B. (登録日: 2025-03-25, 公開日: 2026-02-04, 最終更新日: 2026-03-25)

主引用文献

Bhattacharjee, B.,Noviello, C.M.,Rahman, M.M.,Mayer, J.P.,Gajewiak, J.,McIntosh, J.M.,Hibbs, R.E.,Stowell, M.H.B.
Shape-shifting conotoxins reveal divergent pore-targeting mechanisms in nicotinic receptors.
Structure, 34:463-, 2026

PubMed Abstract: The neuronal α7 nicotinic acetylcholine receptor (α7-nAChR) and muscle-type nicotinic acetylcholine receptor (mt-nAChR) are pivotal in synaptic signaling within the brain and the neuromuscular junction respectively. Additionally, they are both targets of a wide range of drugs and toxins. Here, we utilize cryo-EM to delineate structures of these nAChRs in complex with the conotoxins ImI and ImII from Conus imperialis. Despite nominal sequence differences, ImI and ImII exhibit discrete binding preferences and adopt drastically different conformational states upon binding. ImI engages the orthosteric sites of α7-nAChR, while ImII forms distinct pore-bound complexes with both α7-nAChR and mt-nAChR. Strikingly, ImII adopts a compact globular conformation that binds as a monomer to the α7-nAChR pore and as an oblate dimer to the mt-nAChR pore. These structures advance our understanding of nAChR-ligand interactions and the subtle sequence variations that result in dramatically altered functional outcomes in small peptide toxins.

PubMed: 41468893
DOI: 10.1016/j.str.2025.12.003

実験手法

ELECTRON MICROSCOPY (3.06 Å)