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SUMMARY:What can NMR tell us about how a virus enters its host cell? - Ad 
 Bax\, NIH
DTSTART:20140410T100000Z
DTEND:20140410T110000Z
UID:TALK47151@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:The highly conserved N-terminal 23 residues of the HA2 subunit
  of the influenza glycoprotein hemagglutinin are often referred to as the 
 fusion peptide\, and it plays a pivotal role in fusing viral and host-cell
  membranes. At neutral pH\, NMR reveals a tight helical-hairpin structure\
 , stabilized by aliphatic hydrogen bonding and a charge-dipole interaction
 . At low pH\, where the fusion process is triggered\, the peptide transien
 tly visits activated states which are likely to play a pivotal role in for
 mation of the fusion pore\, an essential structure required in the final s
 tage of membrane fusion.  Another critical step in membrane fusion involve
 s the structural switch of the ecto-domain of class I viral fusion protein
 s from a prefusion state\, to a post-fusion 6-helical bundle (6HB).  A "sp
 ring-loaded" mechanism has been invoked to explain this structural transit
 ion and drive membrane fusion. Instead\, we show that the transition invol
 ves disassembly of the ecto-domain through membrane binding\, followed by 
 assembly of 6HB on the membrane following fusion.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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