Ontology highlight
ABSTRACT:
SUBMITTER: Lorieau JL
PROVIDER: S-EPMC3523815 | biostudies-literature | 2012 Dec
REPOSITORIES: biostudies-literature
Lorieau Justin L JL Louis John M JM Schwieters Charles D CD Bax Adriaan A
Proceedings of the National Academy of Sciences of the United States of America 20121119 49
The highly conserved first 23 residues of the influenza hemagglutinin HA2 subunit constitute the fusion domain, which plays a pivotal role in fusing viral and host-cell membranes. At neutral pH, this peptide adopts a tight helical hairpin wedge structure, stabilized by aliphatic hydrogen bonding and charge-dipole interactions. We demonstrate that at low pH, where the fusion process is triggered, the native peptide transiently visits activated states that are very similar to those sampled by a G8 ...[more]