Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles
| Autor: | Qingxin Li, Qiwei Huang, Congbao Kang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: |
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Molecular Magnetic Resonance Spectroscopy QH301-705.5 Detergents Catalysis Protein Structure Secondary Inorganic Chemistry Protein Domains Humans Amino Acid Sequence Physical and Theoretical Chemistry Biology (General) Molecular Biology Nuclear Magnetic Resonance Biomolecular QD1-999 COVID-19 SARS-CoV-2 S-protein transmembrane domain NMR detergent micelles Spectroscopy Micelles Organic Chemistry Cell Membrane General Medicine Computer Science Applications Chemistry Cross-Linking Reagents Spike Glycoprotein Coronavirus |
| Zdroj: | International Journal of Molecular Sciences; Volume 23; Issue 3; Pages: 1040 International Journal of Molecular Sciences, Vol 23, Iss 1040, p 1040 (2022) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms23031040 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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