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PMID: 3681988 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Journal of molecular biology ·Vol. 196 ·No. 4 ·1987-08-20 ·Pages 963-6

de Groot RJ, Luytjes W, Horzinek MC, van der Zeijst BA, Spaan WJ, Lenstra JA

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.

MeSH Terms
Amino Acid Sequence Coronaviridae/metabolism Macromolecular Substances Molecular Sequence Data Protein Conformation Viral Proteins
Chemicals
Macromolecular Substances Viral Proteins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
de Groot R J
Institute of Virology, Veterinary Faculty, University of Utrecht, The Netherlands.
Luytjes W
Horzinek M C
van der Zeijst B A
Spaan W J
Lenstra J A
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Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
DOI
10.1016/0022-2836(87)90422-0
Published
1987-08-20
Pages
963-6
Language
English
Region
England
NLM ID
2985088R
PMCID
PMC7131189
Subset
IM
External Links
PubMed source DOI: 10.1016/0022-2836(87)90422-0 PMC Full Text View journal details
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