title: Structure and function of membrane fusion peptides.
abstract: Membrane fusion peptides are highly conserved hydrophobic domains of fusion proteins that insert into membranes during membrane fusion. Recent success with solving the structures of the influenza hemagglutinin fusion peptide and some critical mutants of this peptide in membrane environments at high resolution has led to a new understanding of the mechanism of membrane fusion. This review highlights the structures that have been solved and summarizes recent thermodynamic and spectroscopic studies on the interactions of this interesting class of peptides with lipid bilayers.
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville 22908-0736, USA. lkt2e@virginia.edu
authors.forename: Lukas K
authors.initials: LK
authors.lastname: Tamm
authors.forename: Xing
authors.initials: X
authors.lastname: Han
authors.forename: Yinling
authors.initials: Y
authors.lastname: Li
authors.forename: Alex L
authors.initials: AL
authors.lastname: Lai
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008561:Membrane Fusion; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D019267:Hemagglutinin Glycoproteins, Influenza Virus; D008051:Lipid Bilayers; D010455:Peptides