Resonance assignment of the ligand-free cyclic nucleotide-binding domain from the murine ion channel HCN2

Autor: Dieter Willbold, Sven Schünke, Ulrich Benjamin Kaupp, Claudia Börger, Friederike Winkhaus, Justin Lecher, Matthias Stoldt
Rok vydání: 2014
Předmět:
Zdroj: Journal of Biomolecular NMR
ISSN: 1874-270X
1874-2718
DOI: 10.1007/s12104-014-9583-x
Popis: Hyperpolarization activated and cyclic nucleotide-gated (HCN) ion channels as well as cyclic nucleotide-gated (CNG) ion channels are essential for the regulation of cardiac cells, neuronal excitability, and signaling in sensory cells. Both classes are composed of four subunits. Each subunit comprises a transmembrane region, intracellular N- and C-termini, and a C-terminal cyclic nucleotide-binding domain (CNBD). Binding of cyclic nucleotides to the CNBD promotes opening of both CNG and HCN channels. In case of CNG channels, binding of cyclic nucleotides to the CNBD is sufficient to open the channel. In contrast, HCN channels open upon membrane hyperpolarization and their activity is modulated by binding of cyclic nucleotides shifting the activation potential to more positive values. Although several high-resolution structures of CNBDs from HCN and CNG channels are available, the gating mechanism for murine HCN2 channel, which leads to the opening of the channel pore, is still poorly understood. As part of a structural investigation, here, we report the complete backbone and side chain resonance assignments of the murine HCN2 CNBD with part of the C-linker.
Databáze: OpenAIRE
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