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Characterization of a cyclic nucleotide-activated K(+) channel and its lipid environment by using solid-state NMR spectroscopy
- Source :
- ChemBioChem, 14(14), 1789. Wiley-VCH Verlag, ChemBioChem, ICT FP7 Publications Database, OpenAIRE
- Publication Year :
- 2013
-
Abstract
- Voltage-gated ion channels are large tetrameric multidomain membrane proteins that play crucial roles in various cellular transduction pathways. Because of their large size and domain-related mobility, structural characterization has proved challenging. We analyzed high-resolution solid-state NMR data on different isotope-labeled protein constructs of a bacterial cyclic nucleotide-activated K(+) channel (MlCNG) in lipid bilayers. We could identify the different subdomains of the 4×355 residue protein, such as the voltage-sensing domain and the cyclic nucleotide binding domain. Comparison to ssNMR data obtained on isotope-labeled cell membranes suggests a tight association of negatively charged lipids to the channel. We detected spectroscopic polymorphism that extends beyond the ligand binding site, and the corresponding protein segments have been associated with mutant channel types in eukaryotic systems. These findings illustrate the potential of ssNMR for structural investigations on large membrane-embedded proteins, even in the presence of local disorder.
- Subjects :
- Potassium Channels
Mutant
Lipid Bilayers
010402 general chemistry
01 natural sciences
Biochemistry
03 medical and health sciences
Cyclic nucleotide
chemistry.chemical_compound
Lipid bilayer
Molecular Biology
Nuclear Magnetic Resonance, Biomolecular
Ion channel
030304 developmental biology
0303 health sciences
Carbon Isotopes
Binding Sites
Nitrogen Isotopes
Nucleotides
Organic Chemistry
Recombinant Proteins
0104 chemical sciences
Protein Structure, Tertiary
Crystallography
Membrane
Solid-state nuclear magnetic resonance
Membrane protein
chemistry
13. Climate action
Cyclic nucleotide-binding domain
Biophysics
Molecular Medicine
Subjects
Details
- ISSN :
- 14397633 and 14394227
- Volume :
- 14
- Issue :
- 14
- Database :
- OpenAIRE
- Journal :
- Chembiochem : a European journal of chemical biology
- Accession number :
- edsair.doi.dedup.....fff0f5949735e6502d6329d4731ef584