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='3bkd' size='300' frame='true' align='right' caption='High resolution Crystal structure of Transmembrane domain of M2 protein [Stouffer et al]' />
<applet load='1nyj' size='300' frame='true' align='right' caption='The closed state structure of M2 protein H+ channel by solid state NMR spectroscopy [Nishimura et al]' />
 
== Background ==
== Background ==
The M2 proton channel is a key protein that leads to viral infection [Takeuchi et al]. The M2 proton channel acidifies the viron which allows the viral matrix protein (M1) to disassociate from the ribonucleoprotein (RNP) [wu et al]. This allows the RNP to be transported to the nucleus of the cell [wu et al]. Several recent studies have looked at the effects of amantadine and rimantadine on inhibiting the transfer of protons through the M2 channel [stouffer et al].  It has been found that M2 is resistant to these two drugs in 90% of humans, birds and pigs stouffer et al]. Understanding the structure and function of this proton channel is necessary in solving the resistance problem [stouffer et al].  
The M2 proton channel is a key protein that leads to viral infection [Takeuchi et al]. The M2 proton channel acidifies the viron which allows the viral matrix protein (M1) to disassociate from the ribonucleoprotein (RNP) [wu et al]. This allows the RNP to be transported to the nucleus of the cell [wu et al]. Several recent studies have looked at the effects of amantadine and rimantadine on inhibiting the transfer of protons through the M2 channel [stouffer et al].  It has been found that M2 is resistant to these two drugs in 90% of humans, birds and pigs stouffer et al]. Understanding the structure and function of this proton channel is necessary in solving the resistance problem [stouffer et al].  
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== Central Cavity ==
== Central Cavity ==
<applet load='1nyj' size='300' frame='true' align='right' caption='The closed state structure of M2 protein H+ channel by solid state NMR spectroscopy [Nishimura et al]' />
<applet load='3bkd' size='300' frame='true' align='right' caption='High resolution Crystal structure of Transmembrane domain of M2 protein [Stouffer et al]' />
== pH Gating ==
== pH Gating ==