1VOT

ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH HUPERZINE A

1VOT の概要

• エントリーDOI: 10.2210/pdb1vot/pdb
• 分子名称: ACETYLCHOLINESTERASE, Huperzine A (3 entities in total)
• 機能のキーワード: hydrolase, neurotransmitter cleavage
• 由来する生物種: Torpedo californica (Pacific electric ray)
• 細胞内の位置: Isoform H: Cell membrane; Lipid-anchor, GPI- anchor. Isoform T: Cell membrane; Peripheral membrane protein: P04058
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60978.83

構造登録者

Raves, M.L.,Harel, M.,Silman, I.,Sussman, J.L. (登録日: 1996-06-23, 公開日: 1997-06-16, 最終更新日: 2024-11-13)

主引用文献

Raves, M.L.,Harel, M.,Pang, Y.P.,Silman, I.,Kozikowski, A.P.,Sussman, J.L.
Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.
Nat.Struct.Biol., 4:57-63, 1997

PubMed Abstract: (-)-Huperzine A (HupA) is found in an extract from a club moss that has been used for centuries in Chinese folk medicine. Its action has been attributed to its ability to strongly inhibit acetylcholinesterase (AChE). The crystal structure of the complex of AChE with optically pure HupA at 2.5 A resolution shows an unexpected orientation for the inhibitor with surprisingly few strong direct interactions with protein residues to explain its high affinity. This structure is compared to the native structure of AChE devoid of any inhibitor as determined to the same resolution. An analysis of the affinities of structural analogues of HupA, correlated with their interactions with the protein, shows the importance of individual hydrophobic interactions between HupA and aromatic residues in the active-site gorge of AChE.

PubMed: 8989325
DOI: 10.1038/nsb0197-57

実験手法

X-RAY DIFFRACTION (2.5 Å)