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J Mol Biol. 1987 Aug 20;196(4):963-6.

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

Author information

1
Institute of Virology, Veterinary Faculty, University of Utrecht, The Netherlands.

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.

PMID:
3681988
PMCID:
PMC7131189
DOI:
10.1016/0022-2836(87)90422-0
[Indexed for MEDLINE]
Free PMC Article

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