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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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
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author Cukkemane, Abhishek
Nand, Deepak
Gradmann, Sabine
Weingarth, Markus
Kaupp, U. Benjamin
Baldus, Marc
author_facet Cukkemane, Abhishek
Nand, Deepak
Gradmann, Sabine
Weingarth, Markus
Kaupp, U. Benjamin
Baldus, Marc
author_sort Cukkemane, Abhishek
collection PubMed
description 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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spelling pubmed-34383992012-09-17 Solid-state NMR [(13)C,(15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel Cukkemane, Abhishek Nand, Deepak Gradmann, Sabine Weingarth, Markus Kaupp, U. Benjamin Baldus, Marc Biomol NMR Assign Article 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. Springer Netherlands 2012-02-03 2012 /pmc/articles/PMC3438399/ /pubmed/22302441 http://dx.doi.org/10.1007/s12104-012-9363-4 Text en © The Author(s) 2012 https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Article
Cukkemane, Abhishek
Nand, Deepak
Gradmann, Sabine
Weingarth, Markus
Kaupp, U. Benjamin
Baldus, Marc
Solid-state NMR [(13)C,(15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel
title Solid-state NMR [(13)C,(15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel
title_full Solid-state NMR [(13)C,(15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel
title_fullStr Solid-state NMR [(13)C,(15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel
title_full_unstemmed Solid-state NMR [(13)C,(15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel
title_short Solid-state NMR [(13)C,(15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel
title_sort solid-state nmr [(13)c,(15)n] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel
topic Article
url 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
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