3O9M

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

Summary for 3O9M

• Entry DOI: 10.2210/pdb3o9m/pdb
• Related: 2P0P 2PM8 2WSL
• Descriptor: Cholinesterase, BENZOIC ACID (3 entities in total)
• Functional Keywords: cholinesterase, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P06276
• Total number of polymer chains: 2
• Total formula weight: 130543.24

Authors

Asojo, O.A.,Ngamelue, M.N.,Homma, K.,Lockridge, O. (deposition date: 2010-08-04, release date: 2011-04-13, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.98 Å)