 |
PDBsum entry 2k0g
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Membrane protein
|
PDB id
|
|
|
|
2k0g
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Solution structure of the mesorhizobium loti k1 channel cyclic nucleotide-Binding domain in complex with camp.
|
|
|
Authors
|
|
S.Schünke,
M.Stoldt,
K.Novak,
U.B.Kaupp,
D.Willbold.
|
|
|
Ref.
|
|
Embo Rep, 2009,
10,
729-735.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are
crucial in neuronal excitability and signal transduction of sensory cells. HCN
and CNG channels are activated by binding of cyclic nucleotides to their
intracellular cyclic nucleotide-binding domain (CNBD). However, the mechanism by
which the binding of cyclic nucleotides opens these channels is not well
understood. Here, we report the solution structure of the isolated CNBD of a
cyclic nucleotide-sensitive K(+) channel from Mesorhizobium loti. The protein
consists of a wide anti-parallel beta-roll topped by a helical bundle comprising
five alpha-helices and a short 3(10)-helix. In contrast to the dimeric
arrangement ('dimer-of-dimers') in the crystal structure, the solution structure
clearly shows a monomeric fold. The monomeric structure of the CNBD supports the
hypothesis that the CNBDs transmit the binding signal to the channel pore
independently of each other.
|
|
|
|
|
|
|
