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000005102 0247_ $$2DOI$$a10.1038/embor.2009.68
000005102 0247_ $$2WOS$$aWOS:000267599700015
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000005102 041__ $$aeng
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000005102 084__ $$2WoS$$aBiochemistry & Molecular Biology
000005102 084__ $$2WoS$$aCell Biology
000005102 1001_ $$0P:(DE-Juel1)VDB72730$$aSchünke, S.$$b0$$uFZJ
000005102 245__ $$aSolution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP
000005102 260__ $$aLondon [u.a.]$$bNature Publishing Group$$c2009
000005102 300__ $$a729 - 735
000005102 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000005102 3367_ $$2BibTeX$$aARTICLE
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000005102 3367_ $$2DRIVER$$aarticle
000005102 440_0 $$012322$$aEMBO Reports$$v10$$x1469-221X$$y7
000005102 500__ $$aThis study was supported by a research grant from the Helmholtzgemeinschaft
000005102 520__ $$aCyclic 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.
000005102 536__ $$0G:(DE-Juel1)FUEK443$$2G:(DE-HGF)$$aProgramm Biosoft$$cN03$$x0
000005102 536__ $$0G:(DE-Juel1)FUEK409$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x1
000005102 588__ $$aDataset connected to Web of Science, Pubmed
000005102 650_2 $$2MeSH$$aAlphaproteobacteria: chemistry
000005102 650_2 $$2MeSH$$aCrystallography, X-Ray
000005102 650_2 $$2MeSH$$aCyclic AMP: chemistry
000005102 650_2 $$2MeSH$$aCyclic AMP: metabolism
000005102 650_2 $$2MeSH$$aCyclic Nucleotide-Gated Cation Channels: chemistry
000005102 650_2 $$2MeSH$$aCyclic Nucleotide-Gated Cation Channels: metabolism
000005102 650_2 $$2MeSH$$aModels, Molecular
000005102 650_2 $$2MeSH$$aPotassium Channels: chemistry
000005102 650_2 $$2MeSH$$aPotassium Channels: metabolism
000005102 650_2 $$2MeSH$$aProtein Structure, Secondary
000005102 650_2 $$2MeSH$$aProtein Structure, Tertiary
000005102 650_2 $$2MeSH$$aSolutions
000005102 650_7 $$00$$2NLM Chemicals$$aCyclic Nucleotide-Gated Cation Channels
000005102 650_7 $$00$$2NLM Chemicals$$aPotassium Channels
000005102 650_7 $$00$$2NLM Chemicals$$aSolutions
000005102 650_7 $$060-92-4$$2NLM Chemicals$$aCyclic AMP
000005102 650_7 $$2WoSType$$aJ
000005102 65320 $$2Author$$aNMR solution structure
000005102 65320 $$2Author$$aMloK1
000005102 65320 $$2Author$$aion channels
000005102 65320 $$2Author$$aHCN
000005102 65320 $$2Author$$aCNG
000005102 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b1$$uFZJ
000005102 7001_ $$0P:(DE-Juel1)VDB15802$$aNovak, K.$$b2$$uFZJ
000005102 7001_ $$0P:(DE-Juel1)VDB728$$aKaupp, U. B.$$b3$$uFZJ
000005102 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000005102 773__ $$0PERI:(DE-600)2025376-X$$a10.1038/embor.2009.68$$gVol. 10, p. 729 - 735$$p729 - 735$$q10<729 - 735$$tEMBO reports$$v10$$x1469-221X$$y2009
000005102 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2727438
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000005102 9141_ $$y2009
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