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TitleKinetic and structural evidence for specific DMSO interference with reversible binding of uncharged bis-oximes to hAChE and their reactivation kinetics of OP-hAChE.
Journal, issue, pagesChem. Biol. Interact., Vol. 419, Page 111649-111649, Year 2025
Publish dateMay 14, 2025 (structure data deposition date)
AuthorsKolic, D. / Gerlits, O. / Kucharski, M. / Gorecki, L. / Joiner, N. / Kovalevsky, A. / Radic, Z.
External linksChem. Biol. Interact. / PubMed:40653101
MethodsX-ray diffraction
Resolution2.4 - 2.704 Å
Structure data

PDB-9oms:
X-ray structure of human acetylcholinesterase (hAChE) in complex with bis-oxime reactivator LG-1922
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-9omt:
X-ray structure of paraoxon (POX)-inhibited human acetylcholinesterase (hAChE) in complex with bis-oxime reactivator LG-1922
Method: X-RAY DIFFRACTION / Resolution: 2.704 Å

Chemicals

PDB-1cd5:
GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER

ChemComp-NO3:
NITRATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-DEP:
DIETHYL PHOSPHONATE

PDB-1cda:
Unknown entry

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

Source
  • homo sapiens (human)
KeywordsHYDROLASE / homodimer / reactivator complex / organophosphate-inhibited acetylcholinesterase

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