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

Open access
de Groot, R.J., Luytjes, W., Horzinek, M.C., van der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A.·1987·Journal of Molecular Biology

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 α-helices with predicted lengths of 100 and 50 Å, respectively. It is suggested that, in the spike oligomer. these α-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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Metadata

Authors
de Groot, R. J., Luytjes, W., Horzinek, M. C., van der Zeijst, B. A. M., Spaan, W. J. M., & Lenstra, J. A.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
1987-08
Volume
196
Issue
4
Pages
963-966
ISSN
0022-2836 (ISSN-L)
OpenAlex
W2019945910
Cited by
200
References
0
FWCI
8.32
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Evidence for a coiled-coil structure in the spike proteins of coronaviruses. https://app.cochat.ai/papers/10.1016/0022-2836(87)90422-0
The paper
de Groot, R. J., Luytjes, W., Horzinek, M. C., van der Zeijst, B. A. M., Spaan, W. J. M., & Lenstra, J. A. (1987). Evidence for a coiled-coil structure in the spike proteins of coronaviruses. Journal of Molecular Biology. https://doi.org/10.1016/0022-2836(87)90422-0

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.