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| 001 | 153358 | ||
| 005 | 20210129213728.0 | ||
| 024 | 7 | _ | |a 10.1038/ncomms4106 |2 doi |
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| 024 | 7 | _ | |a pmid:24469021 |2 pmid |
| 024 | 7 | _ | |a 2128/24475 |2 Handle |
| 037 | _ | _ | |a FZJ-2014-02989 |
| 082 | _ | _ | |a 500 |
| 100 | 1 | _ | |a Kowal, Julia |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1 |
| 260 | _ | _ | |a London |c 2014 |b Nature Publishing Group |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1399880815_4104 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Cyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly because of a lack of direct structural information. Here we report ligand-induced conformational changes in full-length MloK1, a cyclic nucleotide-modulated potassium channel from the bacterium Mesorhizobium loti, analysed by electron crystallography and atomic force microscopy. Upon cAMP binding, the cyclic nucleotide-binding domains move vertically towards the membrane, and directly contact the S1–S4 voltage sensor domains. This is accompanied by a significant shift and tilt of the voltage sensor domain helices. In both states, the inner pore-lining helices are in an ‘open’ conformation. We propose a mechanism in which ligand binding can favour pore opening via a direct interaction between the cyclic nucleotide-binding domains and voltage sensors. This offers a simple mechanistic hypothesis for the coupling between ligand gating and voltage sensing in eukaryotic HCN channels. |
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| 700 | 1 | _ | |a Chami, Mohamed |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Baumgartner, Paul |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Arheit, Marcel |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Chiu, Po-Lin |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Rangl, Martina |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Scheuring, Simon |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Schröder, Gunnar F. |0 P:(DE-Juel1)132018 |b 7 |
| 700 | 1 | _ | |a Nimigean, Crina M. |0 P:(DE-HGF)0 |b 8 |e Corresponding Author |
| 700 | 1 | _ | |a Stahlberg, Henning |0 P:(DE-HGF)0 |b 9 |
| 773 | _ | _ | |a 10.1038/ncomms4106 |g Vol. 5 |0 PERI:(DE-600)2553671-0 |p (1-10) 4106 |t Nature Communications |v 5 |y 2014 |x 2041-1723 |
| 856 | 4 | _ | |u http://www.nature.com/ncomms/2014/140128/ncomms4106/full/ncomms4106.html |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/153358/files/FZJ-2014-02989.pdf |y OpenAccess |
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