3LII

Recombinant human acetylcholinesterase

3LII の概要

• エントリーDOI: 10.2210/pdb3lii/pdb
• 関連するPDBエントリー: 1b41 1f8u
• 分子名称: Acetylcholinesterase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: recombinant human acetylcholinesterase, blood group antigen, cell junction, cell membrane, disulfide bond, glycoprotein, gpi-anchor, hydrolase, lipoprotein, membrane, neurotransmitter degradation, nucleus, secreted, serine esterase, synapse
• 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: 120179.09

構造登録者

Dvir, H.,Rosenberry, T.,Harel, M.,Silman, I.,Sussman, J. (登録日: 2010-01-25, 公開日: 2010-03-16, 最終更新日: 2024-11-20)

主引用文献

Dvir, H.,Silman, I.,Harel, M.,Rosenberry, T.L.,Sussman, J.L.
Acetylcholinesterase: From 3D structure to function.
Chem.Biol.Interact, 187:10-22, 2010

PubMed Abstract: By rapid hydrolysis of the neurotransmitter, acetylcholine, acetylcholinesterase terminates neurotransmission at cholinergic synapses. Acetylcholinesterase is a very fast enzyme, functioning at a rate approaching that of a diffusion-controlled reaction. The powerful toxicity of organophosphate poisons is attributed primarily to their potent inhibition of acetylcholinesterase. Acetylcholinesterase inhibitors are utilized in the treatment of various neurological disorders, and are the principal drugs approved thus far by the FDA for management of Alzheimer's disease. Many organophosphates and carbamates serve as potent insecticides, by selectively inhibiting insect acetylcholinesterase. The determination of the crystal structure of Torpedo californica acetylcholinesterase permitted visualization, for the first time, at atomic resolution, of a binding pocket for acetylcholine. It also allowed identification of the active site of acetylcholinesterase, which, unexpectedly, is located at the bottom of a deep gorge lined largely by aromatic residues. The crystal structure of recombinant human acetylcholinesterase in its apo-state is similar in its overall features to that of the Torpedo enzyme; however, the unique crystal packing reveals a novel peptide sequence which blocks access to the active-site gorge.

PubMed: 20138030
DOI: 10.1016/j.cbi.2010.01.042

実験手法

X-RAY DIFFRACTION (3.2 Å)