Oblique membrane insertion of viral fusion peptide probed by neutron diffraction

Download
  1. Get@NRC: Oblique membrane insertion of viral fusion peptide probed by neutron diffraction (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1021/bi000224u
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titleBiochemistry
ISSN0006-2960
Volume39
Issue22
Pages65816585; # of pages: 5
AbstractFusion peptides mimic the membrane fusion activities of the larger viral proteins from which they derive their sequences. A possible mode of activity involves their oblique insertion into lipid bilayers, causing membrane disruption by promoting highly curved hemifusion intermediates, leading to fusion. We have determined the location and orientation of the simian immunodeficiency virus (SIV) fusion peptide in planar lipid bilayers using neutron lamellar diffraction. The helical axis of the peptide adopts an angle of 55 relative to the membrane normal, while it positions itself nearest the lipid bilayer surface. This is the first direct observation of the structural interaction between a fusion peptide and a phospholipid bilayer.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Steacie Institute for Molecular Sciences
Peer reviewedNo
Identifier10052306
NPARC number12328508
Export citationExport as RIS
Report a correctionReport a correction
Record identifierbdfe3643-de7a-4c61-93c2-0dbb46ed03cc
Record created2009-09-10
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)