M2 Proton Channel: Difference between revisions
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<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 == | ||
The M2 proton channel is a key protein that leads to viral infection.<ref name="Takeuchi" /> The M2 proton channel acidifies the virion which allows the viral matrix protein (M1) to disassociate from the ribonucleoprotein (RNP).<ref name="Wu">PMID:12972147 </ref> This allows the RNP to be transported to the nucleus of the cell.<ref name="Wu" /> Several recent studies have looked at the effects of <scene name='User:Sarah_Henke/Sandbox_1/Amantadine/1'>amantadine</scene><ref name="Stouffer">PMID:18235504 </ref> and <scene name='User:Sarah_Henke/Sandbox_1/Rimantadine/1'>rimantadine</scene><ref name="Schnell">PMID:18235503 </ref> on inhibiting the transfer of protons through the M2 channel.<ref name="Stouffer" /> Amantadine is a proton surrogate that competes with protons for binding to His37, the residue involved in the gating mechanism.<ref name="Lear" /> It has been found that M2 is resistant to these two drugs in 90% of humans, birds and pigs.<ref name="Stouffer" /> Understanding the structure and function of this proton channel is necessary in solving the resistance problem.<ref name="Stouffer" /> | The M2 proton channel is a key protein that leads to viral infection.<ref name="Takeuchi" /> The M2 proton channel acidifies the virion which allows the viral matrix protein (M1) to disassociate from the ribonucleoprotein (RNP).<ref name="Wu">PMID:12972147 </ref> This allows the RNP to be transported to the nucleus of the cell.<ref name="Wu" /> Several recent studies have looked at the effects of <scene name='User:Sarah_Henke/Sandbox_1/Amantadine/1'>amantadine</scene>([[Symmetrel]])<ref name="Stouffer">PMID:18235504 </ref> and <scene name='User:Sarah_Henke/Sandbox_1/Rimantadine/1'>rimantadine</scene>([[Flumadine]])<ref name="Schnell">PMID:18235503 </ref> on inhibiting the transfer of protons through the M2 channel.<ref name="Stouffer" /> Amantadine is a proton surrogate that competes with protons for binding to His37, the residue involved in the gating mechanism.<ref name="Lear" /> It has been found that M2 is resistant to these two drugs in 90% of humans, birds and pigs.<ref name="Stouffer" /> Understanding the structure and function of this proton channel is necessary in solving the resistance problem.<ref name="Stouffer" /> | ||
== Structure == | == Structure == | ||