Journal Article

PreJuSER-60126

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Resonance assignment of the cyclic nucleotide binding domain from a cyclic nucleotide-gated K+ channel in complex with cAMP

Schünke, S.FZJ* ; Novak, K. ; Stoldt, M.FZJ* ; Kaupp, U. B.FZJ* ; Willbold, D.FZJ*

2007
Springer Netherlands Dordrecht [u.a.]

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Please use a persistent id in citations: doi:10.1007/s12104-007-9049-5

Abstract: In order to determine the structure of the 15 kDa cyclic nucleotide binding domain of a cyclic nucleotide-activated K(+) channel from Mesorhizobium loti and its interaction with cAMP, nearly complete (1)H, (13)C, and (15)N chemical shifts were assigned.

Keyword(s): Alphaproteobacteria: metabolism (MeSH) ; Amino Acid Sequence (MeSH) ; Carbon Isotopes: chemistry (MeSH) ; Cyclic AMP: chemistry (MeSH) ; Cyclic Nucleotide-Gated Cation Channels: chemistry (MeSH) ; Magnetic Resonance Spectroscopy: methods (MeSH) ; Nitrogen Isotopes: chemistry (MeSH) ; Nuclear Magnetic Resonance, Biomolecular: methods (MeSH) ; Potassium Channels: chemistry (MeSH) ; Protein Binding (MeSH) ; Protein Structure, Tertiary (MeSH) ; Protons (MeSH) ; Carbon Isotopes ; Cyclic Nucleotide-Gated Cation Channels ; Nitrogen Isotopes ; Potassium Channels ; Protons ; Cyclic AMP ; J ; ion channel (auto) ; cyclic nucleotide binding domain (auto) ; heteronuclear NMR (auto) ; resonance assignment (auto) ; cAMP (auto)

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Molekulare Biophysik (INB-2)
2. Zelluläre Biophysik (INB-1)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)

Appears in the scientific report 2007

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