M2 Proton Channel: Difference between revisions
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== Central Cavity == | == Central Cavity == | ||
The hydrophilic residues in each α-helix monomer are oriented towards the pore lumen.<ref name="Wu" /> The <scene name='User:Sarah_Henke/Sandbox_1/Hydrophobic/1'>hydrophobic</scene> residues will be in contact with the membrane | The hydrophilic residues in each α-helix monomer are oriented towards the pore lumen.<ref name="Wu" /> The <scene name='User:Sarah_Henke/Sandbox_1/Hydrophobic/1'>hydrophobic</scene> residues will be in contact with the membrane (Color code= {{Template:ColorKey_Hydrophobic}}). The central cavity of the M2 channel is a water-filled pore that is interrupted at residue His37 in each monomer.<ref name="Lear">PMID:12972146 </ref> Residues His37 and Trp41 play a key role in the gating mechanism. | ||
<applet load='3bkd' size='300' frame='true' align='right' caption='High resolution Crystal structure of Transmembrane domain of M2 protein [Stouffer et al, 2008]' /> | <applet load='3bkd' size='300' frame='true' align='right' caption='High resolution Crystal structure of Transmembrane domain of M2 protein [Stouffer et al, 2008]' /> | ||