M2 Proton Channel: Difference between revisions
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== M2 Proton Channel from ''Influenza'' A Virus == | == M2 Proton Channel from ''Influenza'' A Virus == | ||
<applet load='1nyj' size='300' frame='true' align='right' caption='The closed state structure of M2 protein H+ channel by solid state NMR spectroscopy [Stouffer et al, 2008] | <applet load='1nyj' size='300' frame='true' align='right' caption='The closed state structure of M2 protein H+ channel by solid state NMR spectroscopy. [Stouffer et al, 2008]' /> | ||
== Background == | == Background == | ||
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== Central Cavity == | == Central Cavity == | ||
<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]' /> | ||
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}}). Most of the residues in the M2 channel are hydrophobic except Ser31 Gly34, and His37.<ref name="Wu" /> 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> Mutagenesis studies have found that the residues facing the pore are Val27, Ala30, Ser31, Gly34, His37, Leu38, and Trp41.<ref name="Wu" /> Residues His37 and Trp41 play a key role in the gating mechanism and the selectivity filter.<ref name="Wu" /> | 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}}). Most of the residues in the M2 channel are hydrophobic except Ser31 Gly34, and His37.<ref name="Wu" /> 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> Mutagenesis studies have found that the residues facing the pore are Val27, Ala30, Ser31, Gly34, His37, Leu38, and Trp41.<ref name="Wu" /> Residues His37 and Trp41 play a key role in the gating mechanism and the selectivity filter.<ref name="Wu" /> | ||
