Hauptseite > Publikationsdatenbank > Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP > print |
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024 | 7 | _ | |2 DOI |a 10.1038/embor.2009.68 |
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041 | _ | _ | |a eng |
082 | _ | _ | |a 570 |
084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
084 | _ | _ | |2 WoS |a Cell Biology |
100 | 1 | _ | |a Schünke, S. |b 0 |u FZJ |0 P:(DE-Juel1)VDB72730 |
245 | _ | _ | |a Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP |
260 | _ | _ | |a London [u.a.] |b Nature Publishing Group |c 2009 |
300 | _ | _ | |a 729 - 735 |
336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
336 | 7 | _ | |a ARTICLE |2 BibTeX |
336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
336 | 7 | _ | |a article |2 DRIVER |
440 | _ | 0 | |a EMBO Reports |x 1469-221X |0 12322 |y 7 |v 10 |
500 | _ | _ | |a This study was supported by a research grant from the Helmholtzgemeinschaft |
520 | _ | _ | |a 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. |
536 | _ | _ | |a Programm Biosoft |c N03 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK443 |x 0 |
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588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
650 | _ | 2 | |2 MeSH |a Alphaproteobacteria: chemistry |
650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
650 | _ | 2 | |2 MeSH |a Cyclic AMP: chemistry |
650 | _ | 2 | |2 MeSH |a Cyclic AMP: metabolism |
650 | _ | 2 | |2 MeSH |a Cyclic Nucleotide-Gated Cation Channels: chemistry |
650 | _ | 2 | |2 MeSH |a Cyclic Nucleotide-Gated Cation Channels: metabolism |
650 | _ | 2 | |2 MeSH |a Models, Molecular |
650 | _ | 2 | |2 MeSH |a Potassium Channels: chemistry |
650 | _ | 2 | |2 MeSH |a Potassium Channels: metabolism |
650 | _ | 2 | |2 MeSH |a Protein Structure, Secondary |
650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
650 | _ | 2 | |2 MeSH |a Solutions |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Cyclic Nucleotide-Gated Cation Channels |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Potassium Channels |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Solutions |
650 | _ | 7 | |0 60-92-4 |2 NLM Chemicals |a Cyclic AMP |
650 | _ | 7 | |a J |2 WoSType |
653 | 2 | 0 | |2 Author |a NMR solution structure |
653 | 2 | 0 | |2 Author |a MloK1 |
653 | 2 | 0 | |2 Author |a ion channels |
653 | 2 | 0 | |2 Author |a HCN |
653 | 2 | 0 | |2 Author |a CNG |
700 | 1 | _ | |a Stoldt, M. |b 1 |u FZJ |0 P:(DE-Juel1)VDB21601 |
700 | 1 | _ | |a Novak, K. |b 2 |u FZJ |0 P:(DE-Juel1)VDB15802 |
700 | 1 | _ | |a Kaupp, U. B. |b 3 |u FZJ |0 P:(DE-Juel1)VDB728 |
700 | 1 | _ | |a Willbold, D. |b 4 |u FZJ |0 P:(DE-Juel1)132029 |
773 | _ | _ | |a 10.1038/embor.2009.68 |g Vol. 10, p. 729 - 735 |p 729 - 735 |q 10<729 - 735 |0 PERI:(DE-600)2025376-X |t EMBO reports |v 10 |y 2009 |x 1469-221X |
856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2727438 |
856 | 4 | _ | |u https://juser.fz-juelich.de/record/5102/files/FZJ-5102.pdf |z Published final document. |y Restricted |
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