๐ 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 ฮฑ-helices with predicted lengths of 100 and 50 ร
, respectively. It is suggested that, in the spike oligomer. these ฮฑ-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. ยฉ 1987.
keywords
๐ spike protein (353)
๐ acid sequence (108)
๐ amino acid (454)
๐ acid sequences (44)
๐ membrane protein (93)
author
๐ค de Groot, R. J.
๐ค Luytjes, W.
๐ค Horzinek, M. C.
๐ค van der Zeijst, B. A.M.
๐ค Spaan, W. J.M.
๐ค Lenstra, J. A.
year
โฐ 1987
issn
๐ 00222836
volume
196
number
4
page
963-966
citedbycount
115
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