1MAH

FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX

1MAH の概要

• エントリーDOI: 10.2210/pdb1mah/pdb
• 分子名称: ACETYLCHOLINESTERASE, FASCICULIN 2, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: hydrolase, serine esterase, synapse, venom, toxin, complex (hydrolase-toxin) complex, complex (hydrolase/toxin)
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66754.46

構造登録者

Bourne, Y.,Taylor, P.,Marchot, P. (登録日: 1995-11-21, 公開日: 1996-04-03, 最終更新日: 2024-10-23)

主引用文献

Bourne, Y.,Taylor, P.,Marchot, P.
Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex.
Cell(Cambridge,Mass.), 83:503-512, 1995

PubMed Abstract: The crystal structure of the snake toxin fasciculin, bound to mouse acetylcholinesterase (mAChE), at 3.2 A resolution reveals a synergistic three-point anchorage consistent with the picomolar dissociation constant of the complex. Loop II of fasciculin contains a cluster of hydrophobic residues that interact with the peripheral anionic site of the enzyme and sterically occlude substrate access to the catalytic site. Loop I fits in a crevice near the lip of the gorge to maximize the surface area of contact of loop II at the gorge entry. The fasciculin core surrounds a protruding loop on the enzyme surface and stabilizes the whole assembly. Upon binding of fasciculin, subtle structural rearrangements of AChE occur that could explain the observed residual catalytic activity of the fasciculin-enzyme complex.

PubMed: 8521480
DOI: 10.1016/0092-8674(95)90128-0

実験手法

X-RAY DIFFRACTION (3.2 Å)