Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 6, Issue 2, Pages 225-229Publisher
SPRINGER
DOI: 10.1007/s12104-012-9363-4
Keywords
Cyclic nucleotide-binding domain; Cyclic AMP; Solid-state NMR; Magic-angle Spinning
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Funding
- NWO [700.26.121]
- Seventh Framework Programme [211800]
- FEBS long-term postdoctoral fellowship
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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.
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