User:Amy Kerzmann/Sandbox 1
From Proteopedia
Inhibition of the M2 Channel from Influenza A
Overview of Normal Function:
Influenza A virions bind to host cells via interactions between hemagglutinin and host cell gangliosides (or sialyated proteins), which trigger receptor-mediated endocytosis. As the virion-containing endosomes are acidified during the typical maturation process, hemagglutin undergoes a conformational change that leads to membrane fusion. Simultaneously, the M2 channel is activated by the acidic conditions, permitting the flow of proteins from the endosomal lumen to the inside of the viral envelope. This acidification process enhances the rate of viral uncoating that releases viral RNA and other components into the cytosol of the infected cell. In this manner, the function of the M2 channel is essential for viral infectivity.
Channel Structure:
The M2 proton channel of influenza A is a homotetramer. The central core of this protein is comprised of four transmembrane helices, one from each monomeric subunit.
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Channel Function:
Influenza A virions bind to host cells via interactions between hemagglutinin and gangliosides (or sialyated proteins), which triggers receptor-mediated endocytosis. As the virion-containing endosomes are acidified during their typical maturation process, the M2 channel is activated.
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