Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein
At Bristol · University of Bristol · +5 more institutions
Abstract
Locking down the SARS-CoV-2 spike Many efforts to develop therapies against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are focused on the spike (S) protein trimer that binds to the host receptor. Structures of trimeric S protein show its receptor-binding domain in either an up or a down conformation. Toelzer et al. produced SARS-CoV-2 S in insect cells and determined the structure by cryo–electron microscopy. In their dataset, the closed form was predominant and was stabilized by binding linoleic acid, an essential fatty acid. A similar binding pocket appears to be present in previous highly pathogenic coronaviruses, and past studies suggested links between viral infection and fatty acid…
Citation impact
- FWCI
- 9.99
- Percentile
- 100%
- References
- 65
Authors
16Topics & keywords
- Spike Protein
- Spike (software development)
- Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
- Protein structure
- Chemistry
- Coronavirus disease 2019 (COVID-19)
- Biochemistry
- Medicine
- Good health and well-being
Funding
- OOracle
- WTWellcome TrustAwards: 210701/Z/18/Z, 206181/Z/17/Z, 106115/Z/14/Z, 202904/Z/16/Z
- BSBritish Society for Antimicrobial ChemotherapyAward: BSAC-COVID-30
- UFU.S. Food and Drug AdministrationAward: HHSF223201510104C
- MRMedical Research CouncilAwards: MR/R020566/1, MR/R020566/1
- EAEngineering and Physical Sciences Research CouncilAwards: EP/G042853/1, EP/R029407/1, EP/E022197/1, EP/G002843/1, EP/R511663/1, EP/R013764/1, EP/N024117/1, EP/M022609/1, EP/M015378/1, EP/M022609/1, EP/M027546/1, EP/I030395/1, EP/J010588/1, EP/G007705/1, EP/L000253/1, EP/R013764/1
- BABiotechnology and Biological Sciences Research CouncilAwards: BB/L01386X/1, BB/T017066/1, BB/L018756/1, BB/L01386X/1, BB/R000484/1, BB/K016601/1, BB/P000940/1, BB/R000484/1, BB/P000940/1