Proton Channels: Difference between revisions
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<scene name='Proton_Channels/Gating/1'>His37 and Trp41</scene> are believed to be crucial for pH-dependent gating. | <scene name='Proton_Channels/Gating/1'>His37 and Trp41</scene> are believed to be crucial for pH-dependent gating. | ||
(The collapse and re-expansion of their sidechains is due to the [[Morphs|linear interpolation method]].) | (The collapse and re-expansion of their sidechains is due to the [[Morphs|linear interpolation method]].) Here are His and Trp <scene name='Proton_Channels/Gating/2'>spacefilled</scene>. | ||
Revision as of 05:38, 19 March 2008
The M2 protein of influenza A virus is a proton channel. Its function is essential for productive infection by the virus.
See Category:Proton_channel for a list of all proton channel structures.
In January, 2008, crystallographic and NMR structures were published side by side in Nature for the transmembrane domains of the M2 protein: 3bkd and 2rlf. The former appeared to be in an open conformation blocked by amantadine, while the latter appeared to be in a closed conformation stabilized by rimantadine.
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At right is a linear-interpolation morph between 3BKD and 2RLF, showing the proposed opening and closing of this channel.
In addition to watching the animation as alpha-helical ribbons, it is useful to watch it . Be sure to rotate the molecule to watch the animation from different perspectives!
are believed to be crucial for pH-dependent gating. (The collapse and re-expansion of their sidechains is due to the linear interpolation method.) Here are His and Trp .