4M0F

Structure of human acetylcholinesterase in complex with territrem B

4M0F の概要

• エントリーDOI: 10.2210/pdb4m0f/pdb
• 関連するPDBエントリー: 4M0E
• 分子名称: Acetylcholinesterase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, territrem B, ... (7 entities in total)
• 機能のキーワード: acetylcholinesterase, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 121619.87

構造登録者

Cheung, J.,Gary, E.N.,Shiomi, K.,Rosenberry, T.L. (登録日: 2013-08-01, 公開日: 2013-10-16, 最終更新日: 2024-11-06)

主引用文献

Cheung, J.,Gary, E.N.,Shiomi, K.,Rosenberry, T.L.
Structures of human acetylcholinesterase bound to dihydrotanshinone I and territrem B show peripheral site flexibility.
ACS Med Chem Lett, 4:1091-1096, 2013

PubMed Abstract: Acetylcholinesterase is a critical enzyme that regulates neurotransmission by degrading the neurotransmitter acetylcholine in synapses of the nervous system. It is an important target for both therapeutic drugs that treat Alzheimer's disease and chemical warfare agents that cripple the nervous system and cause death through paralysis. The enzyme has both catalytic and peripheral sites to which inhibitors may bind. Structures of recombinant human acetylcholinesterase in complex with the natural product inhibitors dihydrotanshinone I and territrem B reveal dihydrotanshinone I binding that is specific to only the peripheral site and territrem B binding that spans both sites and distorts the protein backbone in the peripheral site. These inhibitors may function as important molecular templates for therapeutics used for treatment of disease and protection against nerve agents.

PubMed: 24900610
DOI: 10.1021/ml400304w

実験手法

X-RAY DIFFRACTION (2.304 Å)