Solid-state NMR spectroscopy applied to a chimeric potassium channel in lipid bilayers.
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.
Schneider
Robert
R
Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
Ader
Christian
C
Lange
Adam
A
Giller
Karin
K
Hornig
Sönke
S
Pongs
Olaf
O
Becker
Stefan
S
Baldus
Marc
M
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
D002247:Carbon Isotopes; D051664:Kv1.3 Potassium Channel; D008051:Lipid Bilayers; D008823:Micelles; D009587:Nitrogen Isotopes