M2 Proton Channel: Difference between revisions
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== Structure == | == 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/Secondary_struture/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/Secondary_struture/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]. | ||
== Central Cavity == | == Central Cavity == | ||
<applet load='1nyj' size='300' frame='true' align='left' caption='The closed state structure of M2 protein H+ channel by solid state NMR spectroscopy' /> | |||
== pH Gating == | == pH Gating == | ||
