Resonance assignment of the cyclic nucleotide binding domain from a cyclic nucleotide-gated K(+) channel in complex with cAMP.
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.
Schünke
Sven
S
Institut für Neurowissenschaften und Biophysik, Forschungszentrum Jülich, Germany.
Novak
Kerstin
K
Stoldt
Matthias
M
Kaupp
U Benjamin
UB
Willbold
Dieter
D
D020561:Alphaproteobacteria / Q000378:metabolism*; D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D000242:Cyclic AMP / Q000737:chemistry*; D054815:Cyclic Nucleotide-Gated Cation Channels / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D015221:Potassium Channels / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011522:Protons
D002247:Carbon Isotopes; D054815:Cyclic Nucleotide-Gated Cation Channels; D009587:Nitrogen Isotopes; D015221:Potassium Channels; D011522:Protons; D000242:Cyclic AMP