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Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles.
Li, Qingxin; Huang, Qiwei; Kang, Congbao.
  • Li Q; Guangdong Provincial Engineering Laboratory of Biomass High Value Utilization, Institute of Biological and Medical Engineering, Guangdong Academy of Sciences, Guangzhou 510316, China.
  • Huang Q; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR), Singapore 138670, Singapore.
  • Kang C; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR), Singapore 138670, Singapore.
Int J Mol Sci ; 23(3)2022 Jan 18.
Article in English | MEDLINE | ID: covidwho-1625435
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Detergents / Spike Glycoprotein, Coronavirus Type of study: Randomized controlled trials Limits: Humans Language: English Year: 2022 Document Type: Article Affiliation country: Ijms23031040

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Detergents / Spike Glycoprotein, Coronavirus Type of study: Randomized controlled trials Limits: Humans Language: English Year: 2022 Document Type: Article Affiliation country: Ijms23031040