M2 Proton Channel: Difference between revisions

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== Structure ==

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 TM helicies are arranged around the channel pore with an approximate fourfold rotational symmetry [takeuchi et al].

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].

== Central Cavity ==

M2 Proton Channel: Difference between revisions

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 == Structure ==
-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 TM helicies are arranged around the channel pore with an approximate fourfold rotational symmetry [takeuchi et al].
+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].
 == Central Cavity ==