Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects.

Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z
J Biol Chem :101007 (2021 Jul 26)
PMID: 34324828
doi: 10.1016/j.jbc.2021.101007 		Submitted to SASBDB: 2021 Mar 18
Published in SASBDB:

SASDL82 – Human acetylcholinesterase, apo

acetylcholinesteraseacetylcholinesterase experimental SAS data
OTHER model
Sample: Acetylcholinesterase dimer, 120 kDa Homo sapiens protein
Acetylcholinesterase monomer, 60 kDa Homo sapiens protein
Buffer: 50 mM Tris/HCl, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 May 29
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 162 nm3

SASDL92 – Human acetylcholinesterase, covalently bound to paraoxon

acetylcholinesteraseacetylcholinesterase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Acetylcholinesterase dimer, 120 kDa Homo sapiens protein
Acetylcholinesterase monomer, 60 kDa Homo sapiens protein
Buffer: 50 mM Tris/HCl, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 May 29
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 142 nm3