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 to 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. (Neither drug is shown in the morph at right.) 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 spacefilled. Be sure to rotate the molecule with your mouse to watch the animation from different perspectives! His37 and Trp41 are believed to be crucial for pH-dependent gating. (The apparent collapse and re-expansion of their sidechains is an artifact due to the linear interpolation method of morphing.) Here are His and Trp spacefilled. To be explained in a later revision, along with new scenes: 3D structures of ion channelsAdditional ResourcesFor additional information, see: Influenza | ||||||||||||
Eric Martz, David Canner, Michal Harel, Eran Hodis, Joel L. Sussman, Jaime Prilusky, Alexander Berchansky
This page was last modified 16:12, 11 June 2025.