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

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

R J de Groot  1 , W Luytjes, M C Horzinek, B A van der Zeijst, W J Spaan, J A Lenstra
Affiliations

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

R J de Groot et al. J Mol Biol. .

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.

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