title: Unravelling the conformational plasticity of the extracellular domain of a prokaryotic nAChR homologue in solution by NMR.
abstract: Pentameric ligand-gated ion channels (pLGICs) of the Cys loop family are transmembrane glycoproteins implicated in a variety of biological functions. Here, we present a solution NMR study of the extracellular domain of a prokaryotic pLGIC homologue from the bacterium Gloeobacter violaceus that is found to be a monomer in solution.
authors: Department of Pharmacy, University of Patras, GR-26504 Patras, Greece.
authors: Christos T
authors: CT
authors: Chasapis
authors: Aikaterini I
authors: AI
authors: Argyriou
authors: Pierre-Jean
authors: PJ
authors: Corringer
authors: Detlef
authors: D
authors: Bentrop
authors: Georgios A
authors: GA
authors: Spyroulias
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D000458:Cyanobacteria / Q000737:chemistry* / Q000235:genetics; D058466:Cysteine Loop Ligand-Gated Ion Channel Receptors / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011978:Receptors, Nicotinic / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012996:Solutions; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; D058466:Cysteine Loop Ligand-Gated Ion Channel Receptors; D021122:Protein Subunits; D011978:Receptors, Nicotinic; D011994:Recombinant Proteins; D012996:Solutions