User:Amy Kerzmann/Sandbox 4

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(New page: == 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...)
(Replacing page with '== 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 sol...')
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== M2 Proton Channel from ''Influenza'' A Virus ==
== M2 Proton Channel from ''Influenza'' A Virus ==
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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 <ref>PMID:12403618</ref>.
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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 <ref>PMID:12403618</ref>.
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== Background ==
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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 <scene name='User:Sarah_Henke/Sandbox_1/Amantadine/1'>amantadine</scene> [Stouffer et al] and <scene name='User:Sarah_Henke/Sandbox_1/Rimantadine/1'>rimantadine</scene> [Schnell et al] 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 <ref>PMID:18235504</ref>.
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== Structure ==
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The M2 proton channel from influenza A is 97 amino acid residues and forms a 24-residue N-terminal extracellular domain, a 19-residue trans-membrane domain, and a 54-residue C-terminal cytoplasmic domain [wu et al]. The 19-residue TM domain forms the highly selective proton channel [Takashi et al]. Circular dichroism spectra has shown the TM domain to form one α-helix that spans the membrane [wu et al]. By analytical ultracentrifugation, the TM domain is found to form <scene name='User:Sarah_Henke/Sandbox_1/Alpha_hlix/1'>α-helical tetramers</scene>[takeuchi et al]. This tetrameric bundle of the TM domain is found by NMR to be tilted by 25-38° from the channel axis [takeuchi et al]. The trameric helices form a left-handed bundle that resembles a truncated cone [Stouffer et al]. The TM helicies are arranged around the channel pore with an approximate fourfold rotational symmetry [takeuchi et al].
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== Central Cavity ==
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<applet load='3bkd' size='300' frame='true' align='right' caption='High resolution Crystal structure of Transmembrane domain of M2 protein [Stouffer et al]' />
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== pH Gating ==
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== References ==
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<references />
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Revision as of 23:24, 29 September 2009

M2 Proton Channel from Influenza A Virus

PDB ID 1nyj

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Proteopedia Page Contributors and Editors (what is this?)

Amy Kerzmann

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