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000153358 1001_ $$0P:(DE-HGF)0$$aKowal, Julia$$b0
000153358 245__ $$aLigand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1
000153358 260__ $$aLondon$$bNature Publishing Group$$c2014
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000153358 520__ $$aCyclic 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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000153358 7001_ $$0P:(DE-HGF)0$$aChami, Mohamed$$b1
000153358 7001_ $$0P:(DE-HGF)0$$aBaumgartner, Paul$$b2
000153358 7001_ $$0P:(DE-HGF)0$$aArheit, Marcel$$b3
000153358 7001_ $$0P:(DE-HGF)0$$aChiu, Po-Lin$$b4
000153358 7001_ $$0P:(DE-HGF)0$$aRangl, Martina$$b5
000153358 7001_ $$0P:(DE-HGF)0$$aScheuring, Simon$$b6
000153358 7001_ $$0P:(DE-Juel1)132018$$aSchröder, Gunnar F.$$b7
000153358 7001_ $$0P:(DE-HGF)0$$aNimigean, Crina M.$$b8$$eCorresponding Author
000153358 7001_ $$0P:(DE-HGF)0$$aStahlberg, Henning$$b9
000153358 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/ncomms4106$$gVol. 5$$p(1-10) 4106$$tNature Communications$$v5$$x2041-1723$$y2014
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