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024 7 _ |2 pmid
|a pmid:20449776
024 7 _ |2 DOI
|a 10.1007/s12104-010-9231-z
024 7 _ |2 WOS
|a WOS:000282317100007
037 _ _ |a PreJuSER-11494
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biophysics
084 _ _ |2 WoS
|a Spectroscopy
100 1 _ |a Schünke, S.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB72730
245 _ _ |a Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain
260 _ _ |a Dordrecht [u.a.]
|b Springer Netherlands
|c 2010
300 _ _ |a 147 - 150
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
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336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a article
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440 _ 0 |a Biomolecular NMR Assignments
|x 1874-2718
|0 18205
|y 2
|v 4
500 _ _ |a This 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.
520 _ _ |a Cyclic 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.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
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536 _ _ |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|0 G:(DE-Juel1)FUEK505
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Cyclic Nucleotide-Gated Cation Channels: chemistry
650 _ 2 |2 MeSH
|a Nuclear Magnetic Resonance, Biomolecular
650 _ 2 |2 MeSH
|a Nucleotides: metabolism
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Rhizobium: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Cyclic Nucleotide-Gated Cation Channels
650 _ 7 |0 0
|2 NLM Chemicals
|a Nucleotides
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a Ion channels
653 2 0 |2 Author
|a Cyclic nucleotide binding domain
653 2 0 |2 Author
|a CNBD
653 2 0 |2 Author
|a HCN
653 2 0 |2 Author
|a CNG
653 2 0 |2 Author
|a Heteronuclear NMR
700 1 _ |a Lecher, J.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB94799
700 1 _ |a Stoldt, M.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB21601
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 10.1007/s12104-010-9231-z
|g Vol. 4, p. 147 - 150
|p 147 - 150
|q 4<147 - 150
|0 PERI:(DE-600)2388861-1
|t Biomolecular NMR assignments
|v 4
|y 2010
|x 1874-2718
856 7 _ |u http://dx.doi.org/10.1007/s12104-010-9231-z
909 C O |o oai:juser.fz-juelich.de:11494
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|v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
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|v Functional Macromolecules and Complexes
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914 1 _ |y 2010
915 _ _ |0 StatID:(DE-HGF)0030
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920 1 _ |d 31.12.2010
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920 1 _ |0 I:(DE-82)080012_20140620
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