5DTI

Crystal structure of mouse acetylcholinesterase

5DTI の概要

• エントリーDOI: 10.2210/pdb5dti/pdb
• 関連するPDBエントリー: 5DTG 5DTJ
• 分子名称: Acetylcholinesterase (2 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cell junction, synapse. Isoform H: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side: P21836
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 120013.57

構造登録者

Tran, T.H.,Tong, L. (登録日: 2015-09-18, 公開日: 2015-10-21, 最終更新日: 2024-11-20)

主引用文献

Katz, F.S.,Pecic, S.,Tran, T.H.,Trakht, I.,Schneider, L.,Zhu, Z.,Ton-That, L.,Luzac, M.,Zlatanic, V.,Damera, S.,Macdonald, J.,Landry, D.W.,Tong, L.,Stojanovic, M.N.
Discovery of New Classes of Compounds that Reactivate Acetylcholinesterase Inhibited by Organophosphates.
Chembiochem, 16:2205-2215, 2015

PubMed Abstract: Acetylcholinesterase (AChE) that has been covalently inhibited by organophosphate compounds (OPCs), such as nerve agents and pesticides, has traditionally been reactivated by using nucleophilic oximes. There is, however, a clearly recognized need for new classes of compounds with the ability to reactivate inhibited AChE with improved in vivo efficacy. Here we describe our discovery of new functional groups--Mannich phenols and general bases--that are capable of reactivating OPC--inhibited AChE more efficiently than standard oximes and we describe the cooperative mechanism by which these functionalities are delivered to the active site. These discoveries, supported by preliminary in vivo results and crystallographic data, significantly broaden the available approaches for reactivation of AChE.

PubMed: 26350723
DOI: 10.1002/cbic.201500348

実験手法

X-RAY DIFFRACTION (2.003 Å)