Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles

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Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles
Title:
Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles
Journal Title:
International Journal of Molecular Sciences
Keywords:
Publication Date:
19 January 2022
Citation:
Li, Q., Huang, Q., & Kang, C. (2022). Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles. International Journal of Molecular Sciences, 23(3), 1040. https://doi.org/10.3390/ijms23031040
Abstract:
Spike protein of SARS-CoV-2 contains a single-span transmembrane (TM) domain and plays roles in receptor binding, viral attachment and viral entry to the host cells. The TM domain of spike protein is critical for viral infectivity. Herein, the TM domain of spike protein of SARS-CoV-2 was reconstituted in detergent micelles and subjected to structural analysis using solution NMR spectroscopy. The results demonstrate that the TM domain of the protein forms a helical structure in detergent micelles. An unstructured linker is identified between the TM helix and heptapeptide repeat 2 region. The linker is due to the proline residue at position 1213. Side chains of the three tryptophan residues preceding to and within the TM helix important for the function of S-protein might adopt multiple conformations which may be critical for their function. The side chain of W1212 was shown to be exposed to solvent and the side chains of residues W1214 and W1217 are buried in micelles. Relaxation study shows that the TM helix is rigid in solution while several residues have exchanges. The secondary structure and dynamics of the TM domain in this study provide insights into the function of the TM domain of spike protein.
License type:
Attribution 4.0 International (CC BY 4.0)
Funding Info:
This research is supported by core funding from: Experimental Drug Development Centre (EDDC)
Grant Reference no. : N. A.

This research / project is supported by the Ministry of Health’s (MOH) / National Medical Research Council (NMRC) - Open Fund Individual Research Grant
Grant Reference no. : OFIRG19may-0011

Funds from the “Hundred-Talent Program” (Grant Numbers: 2020GDASYL-20200102010 and 2020GDASYL-20200102009) from Guangdong Academy of Sciences, China.
Description:
ISSN:
1422-0067
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