TY  - JOUR
AU  - Schünke, S.
AU  - Lecher, J.
AU  - Stoldt, M.
AU  - Kaupp, U. B.
AU  - Willbold, D.
TI  - Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain
JO  - Biomolecular NMR assignments
VL  - 4
SN  - 1874-2718
CY  - Dordrecht [u.a.]
PB  - Springer Netherlands
M1  - PreJuSER-11494
SP  - 147 - 150
PY  - 2010
N1  - 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.
AB  - 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.
KW  - Cyclic Nucleotide-Gated Cation Channels: chemistry
KW  - Nuclear Magnetic Resonance, Biomolecular
KW  - Nucleotides: metabolism
KW  - Protein Structure, Tertiary
KW  - Rhizobium: metabolism
KW  - Cyclic Nucleotide-Gated Cation Channels (NLM Chemicals)
KW  - Nucleotides (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:20449776
UR  - <Go to ISI:>//WOS:000282317100007
DO  - DOI:10.1007/s12104-010-9231-z
UR  - https://juser.fz-juelich.de/record/11494
ER  -