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Coronaviruses spike glycoprotein endodomains: The sequence and structure‐based comprehensive study
Open accessPublished version of a preprint
Abstract
Any protein's flexibility or region makes it available to interact with many biomolecules in the cell. Specifically, such interactions in viruses help them to perform more functions despite having a smaller genome. Therefore, these flexible regions can be exciting and essential targets to be explored for their role in pathogenicity and therapeutic developments as they achieve essential interactions. In the continuation with our previous study on disordered analysis of SARS‐CoV‐2 spike protein's cytoplasmic tail (CTR), or endodomain, here we have explored the endodomain's disordered potential of six other coronaviruses using multiple bioinformatics approaches and molecular dynamics simulations. Based on the comprehensive analysis of its sequence and structural composition, we report the varying disorder propensity in endodomains of spike proteins of coronaviruses. The observations of this study may help to understand the importance of spike glycoprotein endodomain and creating therapeutic interventions against them.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Disorder and Sequence Repeats in Hub Proteins and Their Implications for Network Evolution
Dosztányi, Z., Chen, J., Dunker, A. K., Simon, I., & Tompa, P. (2006) · Journal of Proteome Research · doi:10.1021/pr060171o · Cited by 341
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Metadata
- Authors
- Kumar, P., Bhardwaj, A., Mukherjee, B., Joshi, R., & Giri, R.
- Affiliations
- Indian Institute of Technology Mandi (IN)
- Corresponding author
- Giri, Rajanish
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2023-10-25
- Volume
- 32
- Issue
- 11
- Pages
- e4804-e4804
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- PMC
- PMC10599102
- OpenAlex
- W4387607370
- Cited by
- 2
- References
- 2
- Citations by year
- 2025: 1 · 2023: 1
- FWCI
- 0.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Protein Science (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Science and Engineering Research Board (CRG/2019/005603)
- Indian Council of Medical Research (52/04/2020/BIO/BMS, 58/6/2020/PHA/BMS)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- cytoplasmic tail, intrinsically disordered regions, molecular dynamics simulation, SARS-CoV-2, therapeutic target
- MeSH terms
- SARS-CoV-2, Glycoproteins, Humans, Molecular Dynamics Simulation, Spike Glycoprotein, Coronavirus
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