Evidence for a coiled-coil structure in the spike proteins of coronaviruses

J Mol Biol. 1987 Aug 20;196(4):963-6. doi: 10.1016/0022-2836(87)90422-0.


The amino acid sequences of the spike proteins from three distantly related coronaviruses have been deduced from cDNA sequences. In the C-terminal half, an homology of about 30% was found, while there was no detectable sequence conservation in the N-terminal regions. Hydrophobic "heptad" repeat patterns indicated the presence of two alpha-helices with predicted lengths of 100 and 50 A, respectively. It is suggested that, in the spike oligomer, these alpha-helices form a complex coiled-coil, resembling the supersecondary structures in two other elongated membrane proteins, the haemagglutinin of influenza virus and the variable surface glycoprotein of trypanosomes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Coronaviridae / metabolism*
  • Macromolecular Substances
  • Molecular Sequence Data
  • Protein Conformation
  • Viral Proteins*


  • Macromolecular Substances
  • Viral Proteins