Structural highlights
Function
[SCN3A_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.
Publication Abstract from PubMed
Peptides representing transmembrane regions of the alpha-subunit of the voltage-gated sodium channel were synthesised and their structures analysed, using 1H NMR and CD, in trifluoroethanol and in dodecylphosphocholine micelles. Sequence analysis suggests that the channel has six regions, S1 to S6, predicted to span the membrane in four homologous domains, designated, I, II, III and IV. Presented here are studies of representatives examples of possible single spanning segments (IS2, IS4, IVS4) and a double spanning segment, IS34, composed of segments IS3 and IS4. In addition, we investigated ISlink56, the putative linker region between segments IS5 and IS6. All of the peptides were found to have predominantly alpha-helical structures in both solvent systems. There was some evidence for bending of the longer helices but there was no discernible evidence for well-defined tertiary structure.
Structural studies of synthetic peptides dissected from the voltage-gated sodium channel.,Doak DG, Mulvey D, Kawaguchi K, Villalain J, Campbell ID J Mol Biol. 1996 May 17;258(4):672-87. PMID:8637001[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Doak DG, Mulvey D, Kawaguchi K, Villalain J, Campbell ID. Structural studies of synthetic peptides dissected from the voltage-gated sodium channel. J Mol Biol. 1996 May 17;258(4):672-87. PMID:8637001 doi:http://dx.doi.org/S0022-2836(96)90278-8
