3O9M

Co-crystallization studies of full length recombinant BChE with cocaine offers insights into cocaine detoxification

3O9M の概要

• エントリーDOI: 10.2210/pdb3o9m/pdb
• 関連するPDBエントリー: 2P0P 2PM8 2WSL
• 分子名称: Cholinesterase, BENZOIC ACID (3 entities in total)
• 機能のキーワード: cholinesterase, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P06276
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 130543.24

構造登録者

Asojo, O.A.,Ngamelue, M.N.,Homma, K.,Lockridge, O. (登録日: 2010-08-04, 公開日: 2011-04-13, 最終更新日: 2024-11-06)

主引用文献

Asojo, O.A.,Ngamelue, M.N.,Homma, K.,Lockridge, O.
Cocrystallization studies of full-length recombinant butyrylcholinesterase (BChE) with cocaine.
Acta Crystallogr.,Sect.F, 67:434-437, 2011

PubMed Abstract: Human butyrylcholinesterase (BChE; EC 3.1.1.8) is a 340 kDa tetrameric glycoprotein that is present in human serum at about 5 mg l(-1) and has well documented therapeutic effects on cocaine toxicity. BChE holds promise as a therapeutic that reduces and finally eliminates the rewarding effects of cocaine, thus weaning an addict from the drug. There have been extensive computational studies of cocaine hydrolysis by BChE. Since there are no reported structures of BChE with cocaine or any of the hydrolysis products, full-length monomeric recombinant wild-type BChE was cocrystallized with cocaine. The refined 3 Å resolution structure appears to retain the hydrolysis product benzoic acid in sufficient proximity to form a hydrogen bond to the active-site Ser198.

PubMed: 21505234
DOI: 10.1107/S1744309111004805

実験手法

X-RAY DIFFRACTION (2.98 Å)