title: Solid-state NMR spectroscopy applied to a chimeric potassium channel in lipid bilayers.
abstract: We show that solid-state NMR can be used to investigate the structure and dynamics of a chimeric potassium channel, KcsA-Kv1.3, in lipid bilayers. Sequential resonance assignments were obtained using a combination of (15)N- (13)C and (13)C- (13)C correlation experiments conducted on fully labeled and reverse-labeled as well as C-terminally truncated samples. Comparison of our results with those from X-ray crystallography and solution-state NMR in micelles on the closely related KcsA K (+) channel provides insight into the mechanism of ion channel selectivity and underlines the important role of the lipid environment for membrane protein structure and function.
authors.affiliation: Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
authors.forename: Robert
authors.initials: R
authors.lastname: Schneider
authors.forename: Christian
authors.initials: C
authors.lastname: Ader
authors.forename: Adam
authors.initials: A
authors.lastname: Lange
authors.forename: Karin
authors.initials: K
authors.lastname: Giller
authors.forename: Sönke
authors.initials: S
authors.lastname: Hornig
authors.forename: Olaf
authors.initials: O
authors.lastname: Pongs
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Marc
authors.initials: M
authors.lastname: Baldus
mesh_terms: D002247:Carbon Isotopes; D018360:Crystallography, X-Ray; D006863:Hydrogen-Ion Concentration; D051664:Kv1.3 Potassium Channel / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008823:Micelles; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D013329:Structure-Activity Relationship
chemical_list: D002247:Carbon Isotopes; D051664:Kv1.3 Potassium Channel; D008051:Lipid Bilayers; D008823:Micelles; D009587:Nitrogen Isotopes