2dci
NMR structure of influenza HA fusion peptide mutant W14A in DPC in pH5
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OverviewOverview
The fusion peptide of influenza hemagglutinin is crucial for cell entry of, this virus. Previous studies showed that this peptide adopts a, boomerang-shaped structure in lipid model membranes at the pH of membrane, fusion. To examine the role of the boomerang in fusion, we changed several, residues proposed to stabilize the kink in this structure and measured, fusion. Among these, mutants E11A and W14A expressed hemagglutinins with, hemifusion and no fusion activities, and F9A and N12A had no effect on, fusion, respectively. Binding enthalpies and free energies of mutant, peptides to model membranes and their ability to perturb lipid bilayer, structures correlated well with the fusion activities of the parent, full-length molecules. The structure of W14A determined by NMR and, site-directed spin labeling features a flexible kink that points out of, the membrane, in sharp contrast to the more ordered boomerang of the, wild-type, which points into the membrane. A specific fixed angle, boomerang structure is thus required to support membrane fusion.
About this StructureAbout this Structure
2DCI is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity., Lai AL, Park H, White JM, Tamm LK, J Biol Chem. 2006 Mar 3;281(9):5760-70. Epub 2005 Dec 28. PMID:16407195
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