%0 Journal Article
%A Cukkemane, A.
%A Grüter, B.
%A Novak, K.
%A Gensch, T.
%A Bönigk, W.
%A Gerharz, T.
%A Kaupp, U. B.
%A Seifert, R.
%T Subunits act independently in a cyclic nucleotide-activated K+ channel
%J EMBO reports
%V 8
%@ 1469-221X
%C London [u.a.]
%I Nature Publishing Group
%M PreJuSER-57477
%P 749 - 755
%D 2007
%Z Record converted from VDB: 12.11.2012
%X Ion channels gated by cyclic nucleotides have crucial roles in neuronal excitability and signal transduction of sensory neurons. Here, we studied ligand binding of a cyclic nucleotide-activated K(+) channel from Mesorhizobium loti and its isolated cyclic nucleotide-binding domain. The channel and the binding domain alone bind cyclic AMP with similar affinity in a non-cooperative manner. The cAMP sensitivities of binding and activation coincide. Thus, each subunit in the tetrameric channel acts independently of the others. The binding and gating properties of the bacterial channel are distinctively different from those of eukaryotic cyclic nucleotide-gated channels.
%K Alphaproteobacteria: metabolism
%K Bacterial Proteins: chemistry
%K Bacterial Proteins: genetics
%K Cyclic AMP: chemistry
%K Cyclic Nucleotide-Gated Cation Channels: chemistry
%K Cyclic Nucleotide-Gated Cation Channels: genetics
%K Ligands
%K Potassium Channels: chemistry
%K Potassium Channels: genetics
%K Protein Structure, Tertiary
%K Protein Subunits: chemistry
%K Spectrometry, Fluorescence
%K Bacterial Proteins (NLM Chemicals)
%K Cyclic Nucleotide-Gated Cation Channels (NLM Chemicals)
%K Ligands (NLM Chemicals)
%K Potassium Channels (NLM Chemicals)
%K Protein Subunits (NLM Chemicals)
%K Cyclic AMP (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:17668006
%2 pmc:PMC1978089
%U <Go to ISI:>//WOS:000248447300011
%R 10.1038/sj.embor.7401025
%U https://juser.fz-juelich.de/record/57477