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
The six-transmembrane helix (6 TM) tetrameric cation channels form the largest ion channel family, some members of which are voltage-gated and others are not. There are no reported channel structures to match the wealth of functional data on the non-voltage-gated members. We determined the structure of the transmembrane regions of the bacterial cyclic nucleotide-regulated channel MlotiK1, a non-voltage-gated 6 TM channel. The structure showed how the S1-S4 domain and its associated linker can serve as a clamp to constrain the gate of the pore and possibly function in concert with ligand-binding domains to regulate the opening of the pore. The structure also led us to hypothesize a new mechanism by which motions of the S6 inner helices can gate the ion conduction pathway at a position along the pore closer to the selectivity filter than the canonical helix bundle crossing.
Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel.,Clayton GM, Altieri S, Heginbotham L, Unger VM, Morais-Cabral JH Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1511-5. Epub 2008 Jan 23. PMID:18216238[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, Altieri S, Heginbotham L, Unger VM, Morais-Cabral JH. Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel. Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1511-5. Epub 2008 Jan 23. PMID:18216238
