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

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-sta...

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Detalles Bibliográficos
Autores principales: Cukkemane, Abhishek, Nand, Deepak, Gradmann, Sabine, Weingarth, Markus, Kaupp, U. Benjamin, Baldus, Marc
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3438399/
https://www.ncbi.nlm.nih.gov/pubmed/22302441
http://dx.doi.org/10.1007/s12104-012-9363-4
Descripción
Sumario: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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s12104-012-9363-4) contains supplementary material, which is available to authorized users.

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