6533b854fe1ef96bd12aeb1b

RESEARCH PRODUCT

Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein

Puig MoraMaría J. GómaraIsmael MingarroJosé L. Nieva

subject

Circular dichroismEbola glycoproteinProtein insertion into membranesProlinePeptide conformationMutantMolecular Sequence DataBiophysicsBiochemistrySendai viruschemistry.chemical_compoundStructural BiologyGeneticsProlineAmino Acid SequenceMolecular BiologyPeptide sequencePOPCchemistry.chemical_classificationChemistryProteïnes de membranaCell BiologyEbolavirusFusion proteinPeptide FragmentsPeptide ConformationViral fusion peptideBiochemistryAvian Sarcoma VirusesLiposomesHIV-1PèptidsGlycoproteinPeptide–lipid interactionViral Fusion Proteins

description

AbstractThe structural determinants underlying the functionality of viral internal fusion peptides (IFPs) are not well understood. We have compared EBOwt (GAAIGLAWIPYFGPAAE), representing the IFP of the Ebola fusion protein GP, and EBOmut (GAAIGLAWIPYFGRAAE) derived from a non-functional mutant with conserved Pro537 substituted by Arg. P537R substitution did not abrogate peptide-membrane association, but interfered with the ability to induce bilayer destabilization. Structural determinations suggest that Pro537 is required to preserve a membrane-perturbing local conformation in apolar environments.

yearjournalcountryeditionlanguage
2004-01-01FEBS Letters
10.1016/j.febslet.2004.06.006http://dx.doi.org/10.1016/j.febslet.2004.06.006