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000016576 0247_ $$2pmc$$apmc:PMC3076860
000016576 0247_ $$2DOI$$a10.1073/pnas.1015890108
000016576 0247_ $$2WOS$$aWOS:000289413600042
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000016576 084__ $$2WoS$$aMultidisciplinary Sciences
000016576 1001_ $$0P:(DE-Juel1)VDB72730$$aSchünke, S.$$b0$$uFZJ
000016576 245__ $$aStructural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel
000016576 260__ $$aWashington, DC$$bAcademy$$c2011
000016576 300__ $$a6121 - 6126
000016576 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000016576 3367_ $$00$$2EndNote$$aJournal Article
000016576 3367_ $$2BibTeX$$aARTICLE
000016576 3367_ $$2ORCID$$aJOURNAL_ARTICLE
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000016576 440_0 $$05100$$aProceedings of the National Academy of Sciences of the United States of America$$v108$$x0027-8424$$y15
000016576 500__ $$aThis study was supported by a fellowship from the International Research School BioStruct to S.S. and a research grant from the Helmholtz-Gemeinschaft (Virtual Institute of Structural Biology) to D.W.
000016576 520__ $$aCyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are activated by binding of ligands to a domain (CNBD) located on the cytoplasmic side of the channel. The underlying mechanisms are not well understood. To elucidate the gating mechanism, structures of both the ligand-free and -bound CNBD are required. Several crystal structures of the CNBD from HCN2 and a bacterial CNG channel (MloK1) have been solved. However, for HCN2, the cAMP-free and -bound state did not reveal substantial structural rearrangements. For MloK1, structural information for the cAMP-free state has only been gained from mutant CNBDs. Moreover, in the crystal, the CNBD molecules form an interface between dimers, proposed to be important for allosteric channel gating. Here, we have determined the solution structure by NMR spectroscopy of the cAMP-free wild-type CNBD of MloK1. A comparison of the solution structure of cAMP-free and -bound states reveals large conformational rearrangement on ligand binding. The two structures provide insights on a unique set of conformational events that accompany gating within the ligand-binding site.
000016576 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000016576 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000016576 588__ $$aDataset connected to Web of Science, Pubmed
000016576 650_2 $$2MeSH$$aAlphaproteobacteria: metabolism
000016576 650_2 $$2MeSH$$aCrystallography, X-Ray
000016576 650_2 $$2MeSH$$aCyclic AMP: chemistry
000016576 650_2 $$2MeSH$$aCyclic Nucleotide-Gated Cation Channels: chemistry
000016576 650_2 $$2MeSH$$aCyclic Nucleotide-Gated Cation Channels: genetics
000016576 650_2 $$2MeSH$$aMutation
000016576 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000016576 650_2 $$2MeSH$$aProtein Structure, Tertiary
000016576 650_7 $$00$$2NLM Chemicals$$aCyclic Nucleotide-Gated Cation Channels
000016576 650_7 $$060-92-4$$2NLM Chemicals$$aCyclic AMP
000016576 650_7 $$2WoSType$$aJ
000016576 65320 $$2Author$$aNMR solution structure
000016576 65320 $$2Author$$aapo state
000016576 65320 $$2Author$$aligand removal method
000016576 65320 $$2Author$$apotassium channel
000016576 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b1$$uFZJ
000016576 7001_ $$0P:(DE-Juel1)VDB94799$$aLecher, J.$$b2$$uFZJ
000016576 7001_ $$0P:(DE-HGF)0$$aKaupp, U.B.$$b3
000016576 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000016576 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.1015890108$$gVol. 108, p. 6121 - 6126$$p6121 - 6126$$q108<6121 - 6126$$tProceedings of the National Academy of Sciences of the United States of America$$v108$$x0027-8424$$y2011
000016576 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3076860
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000016576 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x1
000016576 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
000016576 9141_ $$y2011
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