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Recombinant extracellular domains of human neuronal nicotinic receptors: Preliminary studies on mutant forms for the improvement of solubility

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dc.contributor.author Zouridakis, M en
dc.contributor.author Zisimopoulou, P en
dc.contributor.author Eliopoulos, E en
dc.contributor.author Jacobson, L en
dc.contributor.author Poulas, K en
dc.contributor.author Tzartos, SJ en
dc.date.accessioned 2014-06-06T06:48:02Z
dc.date.available 2014-06-06T06:48:02Z
dc.date.issued 2007 en
dc.identifier.issn 00902977 en
dc.identifier.uri http://dx.doi.org/10.1007/s11062-007-0036-3 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/3921
dc.subject α7 neuronal acetylcholine receptor en
dc.subject Circular dichroism spectroscopy en
dc.subject Extracellular domain en
dc.subject Molecular modeling en
dc.title Recombinant extracellular domains of human neuronal nicotinic receptors: Preliminary studies on mutant forms for the improvement of solubility en
heal.type conferenceItem en
heal.identifier.primary 10.1007/s11062-007-0036-3 en
heal.publicationDate 2007 en
heal.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. © 2007 Springer Science+Business Media, Inc. en
heal.journalName Neurophysiology en
dc.identifier.issue 4-5 en
dc.identifier.volume 39 en
dc.identifier.doi 10.1007/s11062-007-0036-3 en
dc.identifier.spage 259 en
dc.identifier.epage 263 en


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