Structural highlights
Function
CNGK1_RHILO Cyclic nucleotide-regulated potassium channel activated by cAMP.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Here we describe the initial functional characterization of a cyclic nucleotide regulated ion channel from the bacterium Mesorhizobium loti and present two structures of its cyclic nucleotide binding domain, with and without cAMP. The domains are organized as dimers with the interface formed by the linker regions that connect the nucleotide binding pocket to the pore domain. Together, structural and functional data suggest the domains form two dimers on the cytoplasmic face of the channel. We propose a model for gating in which ligand binding alters the structural relationship within a dimer, directly affecting the position of the adjacent transmembrane helices.
Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel.,Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH Cell. 2004 Nov 24;119(5):615-27. PMID:15550244[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell. 2004 Nov 24;119(5):615-27. PMID:15550244 doi:10.1016/j.cell.2004.10.030
- ↑ Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell. 2004 Nov 24;119(5):615-27. PMID:15550244 doi:10.1016/j.cell.2004.10.030
