TY  - JOUR
AU  - Schünke, S.
AU  - Stoldt, M.
AU  - Novak, K.
AU  - Kaupp, U. B.
AU  - Willbold, D.
TI  - Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP
JO  - EMBO reports
VL  - 10
SN  - 1469-221X
CY  - London [u.a.]
PB  - Nature Publishing Group
M1  - PreJuSER-5102
SP  - 729 - 735
PY  - 2009
N1  - This study was supported by a research grant from the Helmholtzgemeinschaft
AB  - Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are crucial in neuronal excitability and signal transduction of sensory cells. HCN and CNG channels are activated by binding of cyclic nucleotides to their intracellular cyclic nucleotide-binding domain (CNBD). However, the mechanism by which the binding of cyclic nucleotides opens these channels is not well understood. Here, we report the solution structure of the isolated CNBD of a cyclic nucleotide-sensitive K(+) channel from Mesorhizobium loti. The protein consists of a wide anti-parallel beta-roll topped by a helical bundle comprising five alpha-helices and a short 3(10)-helix. In contrast to the dimeric arrangement ('dimer-of-dimers') in the crystal structure, the solution structure clearly shows a monomeric fold. The monomeric structure of the CNBD supports the hypothesis that the CNBDs transmit the binding signal to the channel pore independently of each other.
KW  - Alphaproteobacteria: chemistry
KW  - Crystallography, X-Ray
KW  - Cyclic AMP: chemistry
KW  - Cyclic AMP: metabolism
KW  - Cyclic Nucleotide-Gated Cation Channels: chemistry
KW  - Cyclic Nucleotide-Gated Cation Channels: metabolism
KW  - Models, Molecular
KW  - Potassium Channels: chemistry
KW  - Potassium Channels: metabolism
KW  - Protein Structure, Secondary
KW  - Protein Structure, Tertiary
KW  - Solutions
KW  - Cyclic Nucleotide-Gated Cation Channels (NLM Chemicals)
KW  - Potassium Channels (NLM Chemicals)
KW  - Solutions (NLM Chemicals)
KW  - Cyclic AMP (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:19465888
C2  - pmc:PMC2727438
UR  - <Go to ISI:>//WOS:000267599700015
DO  - DOI:10.1038/embor.2009.68
UR  - https://juser.fz-juelich.de/record/5102
ER  -