title: Evidence for a coiled-coil structure in the spike proteins of coronaviruses.
abstract: 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.
authors: Institute of Virology, Veterinary Faculty, University of Utrecht, The Netherlands.
authors: R J
authors: RJ
authors: de Groot
authors: W
authors: W
authors: Luytjes
authors: M C
authors: MC
authors: Horzinek
authors: B A
authors: BA
authors: van der Zeijst
authors: W J
authors: WJ
authors: Spaan
authors: J A
authors: JA
authors: Lenstra
mesh_terms: D000595:Amino Acid Sequence; D003332:Coronaviridae / Q000378:metabolism*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014764:Viral Proteins
chemical_list: D046911:Macromolecular Substances; D014764:Viral Proteins