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