Sandbox Reserved 695: Difference between revisions

For better illustration of the structures at work, the structure shown will only contain one subunit. The <scene name='Sandbox_Reserved_695/Vgsc_alphabeta/2'>secondary structure</scene> includes alpha helices (blue) and beta strands (red). The <scene name='Sandbox_Reserved_695/Vgsc_hydrophobicpolar/2'>hydrophobicity</scene> of the structure reveals that the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Polar}} residues are not exactly easy to illustrate in their membrane bound and subunit bound region.,  but the somewhat diffuse polar regions of the molecule are instrumental in providing the channel with enough hydrophillic residues to allow the passage of ions without allowing significant passage of solvent. In coordination with the hydrophobicity illustration, the <scene name='Sandbox_Reserved_695/Vgsc_evolutionaryconservation/2'>evolutionary conservation</scene> plot shows that both some of the hydrophobic and hydrophillic residues are highly conserved {{Template:ColorKey_ConSurf_NoYellow}}.

The channel protein mostly interacts with sodium ions under normal circumstances, but the activity of the antiepileptic drugs is obviously and important exception to be considered. The sodium ions are conveyed through the channel by favorable interactions with the <scene name='Sandbox_Reserved_695/Vgsc_anionic/1'>anionic redidues</scene>, in particular, the <font color='red'>glutamic acid residues</font> that line the channel helix.