Membrane Structures of the Hemifusion-Inducing Fusion Peptide Mutant G1S and the Fusion-Blocking Mutant G1V of Influenza Virus Hemagglutinin Suggest a Mechanism for Pore Opening in Membrane Fusion

Influenza virus hemagglutinin (HA)-mediated membrane fusion is initiated by a conformational change that releases a V-shaped hydrophobic fusion domain, the fusion peptide, into the lipid bilayer of the target membrane. The most N-terminal residue of this domain, a glycine, is highly conserved and is...

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Main Authors: Li, Yinling, Han, Xing, Lai, Alex L., Bushweller, John H., Cafiso, David S., Tamm, Lukas K.
Formato: Artigo
Idioma:Inglês
Publicado: American Society for Microbiology 2005
Assuntos:
Structure and Assembly
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC1212637/
https://ncbi.nlm.nih.gov/pubmed/16140782
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.79.18.12065-12076.2005
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