Structural highlights
Function
[SCN2A_RAT] Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.
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 sodium channel initiates action potentials by opening in response to membrane depolarization. Fast channel inactivation, which is required for proper physiological function, is mediated by a cytoplasmic loop proposed to occlude the ion pore via a hinged lid mechanism with the triad IFM serving as a hydrophobic "latch". The NMR solution structure of the isolated inactivation gate reveals a stably folded core comprised of an alpha-helix capped by an N-terminal turn, supporting a model in which the tightly folded core containing the latch motif pivots on a more flexible hinge region to occlude the pore during inactivation. The structure, in combination with substituted cysteine mutagenesis experiments, indicates that the IFM triad and adjacent Thr are essential components of the latch and suggests differing roles for the residues of the IFMT motif in fast inactivation.
Solution structure of the sodium channel inactivation gate.,Rohl CA, Boeckman FA, Baker C, Scheuer T, Catterall WA, Klevit RE Biochemistry. 1999 Jan 19;38(3):855-61. PMID:9893979[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rohl CA, Boeckman FA, Baker C, Scheuer T, Catterall WA, Klevit RE. Solution structure of the sodium channel inactivation gate. Biochemistry. 1999 Jan 19;38(3):855-61. PMID:9893979 doi:http://dx.doi.org/10.1021/bi9823380
