Solid-state NMR [13C,15N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel

Biomol NMR Assign. 2012 Oct;6(2):225-9. doi: 10.1007/s12104-012-9363-4.


Channels regulated by cyclic nucleotides are key signalling proteins in several biological pathways. The regulatory aspect is conferred by a C-terminal cyclic nucleotide-binding domain (CNBD). We report resonance assignments of the CNBD of a bacterial mlCNG channel obtained using 2D and 3D solid-state NMR under Magic-angle Spinning conditions. A secondary chemical shift analysis of the 141 residue protein suggests a three-dimensional fold seen in earlier X-ray and solution-state NMR work and points to spectroscopic polymorphism for a selected set of resonances.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Carbon Isotopes
  • Cyclic Nucleotide-Gated Cation Channels / chemistry*
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Nucleotides / metabolism*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary


  • Bacterial Proteins
  • Carbon Isotopes
  • Cyclic Nucleotide-Gated Cation Channels
  • Nitrogen Isotopes
  • Nucleotides