Heptad-repeat regions of respiratory syncytial virus F1 protein form a six-membered coiled-coil complex

Biochemistry. 2000 Sep 26;39(38):11684-95. doi: 10.1021/bi000471y.


The Respiratory Syncytial Virus (RSV) fusogenic glycoprotein F(1) was characterized using biochemical and biophysical techniques. Two heptad-repeat (HR) regions within F(1) were shown to interact. Proteinase-K digestion experiments highlight the HR1 region (located proximal to the fusion peptide sequence) of the F(1) protein to which an HR2-derived (located proximal to the membrane-spanning domain) peptide binds, thus protecting both the protein and peptide from digestion. Solution-phase analysis of HR1-derived peptides shows that these peptides adopt helical secondary structure as measured by circular dichroism. Sedimentation equilibrium studies indicate that these HR1 peptides self-associate in a monomer/trimer equilibrium with an association constant of 5.2 x 10(8) M(-2). In contrast, HR2-derived peptides form random monomers in solution. CD analysis of mixtures containing peptides from the two regions demonstrate their propensity to interact and form a very stable (T(m) = 87 degrees C), helical (86% helicity) complex comprised of three HR1 and three HR2 members.

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Endopeptidase K
  • HN Protein*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Protein Binding / genetics
  • Protein Structure, Secondary / genetics
  • Protein Structure, Tertiary / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Repetitive Sequences, Amino Acid* / genetics
  • Respiratory Syncytial Virus, Human / chemistry*
  • Respiratory Syncytial Virus, Human / genetics
  • Ultracentrifugation
  • Viral Envelope Proteins
  • Viral Fusion Proteins / chemistry*
  • Viral Fusion Proteins / genetics
  • Viral Fusion Proteins / metabolism
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism


  • HN Protein
  • Peptide Fragments
  • Recombinant Proteins
  • Viral Envelope Proteins
  • Viral Fusion Proteins
  • Viral Proteins
  • attachment protein G
  • Endopeptidase K