Abstract
An extracellular domain (ECD) of the human α7 neuronal nicotinic acetylcholine receptor (nAChR) is implicated in a series of neurological disorders. To facilitate structural studies of this domain essential for rational drug design, we designed and expressed mutated forms of human α7 ECD in yeast Pichia pastoris. The novel mutations were based on a model we constructed for α7 ECD using crystal and electron microscopy structures of the homologous invertebrate ACh-binding protein and the Torpedo nAChR, respectively. Preliminary biochemical and physicochemical data indicated that we obtained at least one α7 ECD mutant with proper folding and increased solubility (compared to the wild-type ECD) promising for detailed structural studies.
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Neirofiziologiya/Neurophysiology, Vol. 39, Nos. 4/5, pp. 302–306, July–October, 2007.
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Zouridakis, M., Zisimopoulou, P., Eliopoulos, E. et al. Recombinant extracellular domains of human neuronal nicotinic receptors: Preliminary studies on mutant forms for the improvement of solubility. Neurophysiology 39, 259–263 (2007). https://doi.org/10.1007/s11062-007-0036-3
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DOI: https://doi.org/10.1007/s11062-007-0036-3