TY - JOUR
T1 - Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus
AU - Wang, Jun
AU - Qiu, Jade Xiaoyan
AU - Soto, Cinque
AU - Degrado, William F.
N1 - Funding Information:
This work was funded by the NIH (GM56423 and AI74571). The authors would like to thank Gevorg Grigoryan and Nate Joh for valuable comments and help with preparing the figures.
PY - 2011/2
Y1 - 2011/2
N2 - The M2 proton channel from influenza A virus, a prototype for a class of viral ion channels known as viroporins, conducts protons along a chain of water molecules and ionizable sidechains, including His37. Recent studies highlight a delicate interplay between protein folding, proton binding, and proton conduction through the channel. Drugs inhibit proton conduction by binding to an aqueous cavity adjacent to M2's proton-selective filter, thereby blocking access of proton to the filter, and altering the energetic landscape of the channel and the energetics of proton-binding to His37.
AB - The M2 proton channel from influenza A virus, a prototype for a class of viral ion channels known as viroporins, conducts protons along a chain of water molecules and ionizable sidechains, including His37. Recent studies highlight a delicate interplay between protein folding, proton binding, and proton conduction through the channel. Drugs inhibit proton conduction by binding to an aqueous cavity adjacent to M2's proton-selective filter, thereby blocking access of proton to the filter, and altering the energetic landscape of the channel and the energetics of proton-binding to His37.
UR - http://www.scopus.com/inward/record.url?scp=79551687044&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79551687044&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2010.12.002
DO - 10.1016/j.sbi.2010.12.002
M3 - Review article
C2 - 21247754
AN - SCOPUS:79551687044
SN - 0959-440X
VL - 21
SP - 68
EP - 80
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 1
ER -