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000011494 084__ $$2WoS$$aBiophysics
000011494 084__ $$2WoS$$aSpectroscopy
000011494 1001_ $$0P:(DE-Juel1)VDB72730$$aSchünke, S.$$b0$$uFZJ
000011494 245__ $$aResonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain
000011494 260__ $$aDordrecht [u.a.]$$bSpringer Netherlands$$c2010
000011494 300__ $$a147 - 150
000011494 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000011494 440_0 $$018205$$aBiomolecular NMR Assignments$$v4$$x1874-2718$$y2
000011494 500__ $$aThis work was supported by a fellowship from the International Research School "BioStruct'' to S. Schunke and a research grant from the Helmholtz-Gemeinschaft ("Virtual Institute of Structural Biology'') to D. Willbold.
000011494 520__ $$aCyclic nucleotide-sensitive ion channels, known as HCN and CNG channels play crucial roles in neuronal excitability and signal transduction of sensory cells. These channels are activated by binding of cyclic nucleotides to their intracellular cyclic nucleotide-binding domain (CNBD). A comparison of the structures of wildtype ligand-free and ligand-bound CNBD is essential to elucidate the mechanism underlying nucleotide-dependent activation of CNBDs. We recently reported the solution structure of the Mesorhizobium loti K1 (MloK1) channel CNBD in complex with cAMP. We have now extended these studies and achieved nearly complete assignments of (1)H, (13)C and (15)N resonances of the nucleotide-free CNBD. A completely new assignment of the nucleotide-free wildtype CNBD was necessary due to the sizable chemical shift differences as compared to the cAMP bound CNBD and the slow exchange behaviour between both forms. Scattering of these chemical shift differences over the complete CNBD suggests that nucleotide binding induces significant overall conformational changes.
000011494 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000011494 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000011494 588__ $$aDataset connected to Web of Science, Pubmed
000011494 650_2 $$2MeSH$$aCyclic Nucleotide-Gated Cation Channels: chemistry
000011494 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000011494 650_2 $$2MeSH$$aNucleotides: metabolism
000011494 650_2 $$2MeSH$$aProtein Structure, Tertiary
000011494 650_2 $$2MeSH$$aRhizobium: metabolism
000011494 650_7 $$00$$2NLM Chemicals$$aCyclic Nucleotide-Gated Cation Channels
000011494 650_7 $$00$$2NLM Chemicals$$aNucleotides
000011494 650_7 $$2WoSType$$aJ
000011494 65320 $$2Author$$aIon channels
000011494 65320 $$2Author$$aCyclic nucleotide binding domain
000011494 65320 $$2Author$$aCNBD
000011494 65320 $$2Author$$aHCN
000011494 65320 $$2Author$$aCNG
000011494 65320 $$2Author$$aHeteronuclear NMR
000011494 7001_ $$0P:(DE-Juel1)VDB94799$$aLecher, J.$$b1$$uFZJ
000011494 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b2$$uFZJ
000011494 7001_ $$0P:(DE-Juel1)VDB728$$aKaupp, U. B.$$b3$$uFZJ
000011494 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000011494 773__ $$0PERI:(DE-600)2388861-1$$a10.1007/s12104-010-9231-z$$gVol. 4, p. 147 - 150$$p147 - 150$$q4<147 - 150$$tBiomolecular NMR assignments$$v4$$x1874-2718$$y2010
000011494 8567_ $$uhttp://dx.doi.org/10.1007/s12104-010-9231-z
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000011494 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x1
000011494 9132_ $$0G:(DE-HGF)POF3-551$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft  Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vFunctional Macromolecules and Complexes$$x0
000011494 9141_ $$y2010
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