Proton Channels: Difference between revisions
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In January, 2008, crystallographic and NMR structures were published side by side 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. | In January, 2008, crystallographic and NMR structures were published side by side 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. | ||
At right is a linear-interpolation morph between 3BKD and 2RLF, showing the proposed opening and closing of this channel. | At right is a linear-interpolation morph between 3BKD and 2RLF, showing the proposed opening and closing of this channel. (Controls for animating this morph are under development.) | ||
Revision as of 21:04, 14 March 2008
The M2 protein of influenza A virus is a proton channel. Its function is essential to infection by the virus.
In January, 2008, crystallographic and NMR structures were published side by side 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.
At right is a linear-interpolation morph between 3BKD and 2RLF, showing the proposed opening and closing of this channel. (Controls for animating this morph are under development.)
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Eric Martz, David Canner, Michal Harel, Eran Hodis, Joel L. Sussman, Jaime Prilusky, Alexander Berchansky
