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Met58 and di-acidic motif located at C-terminal region of SARS-CoV-2 ORF6 plays a crucial role in its structural conformations
Open accessPreprint — published as 10.1016/j.bpc.2024.107384 · Paper page
Abstract
Despite being mostly neglected in structural biology, the C-terminal Regions (CTRs) are studied to be multifunctional in humans as well as in viruses. Their role in cellular processes such as trafficking, protein-protein interactions, and protein-lipid interactions are known due to their structural properties. In our previous findings on SARS-CoV-2 Spike and NSP1 proteins, the C-terminal regions (CTRs) are observed to be disordered and experimental evidence showed a gain of structure properties in different physiological environments. In this line, we have investigated the structural dynamics of CTR (residues 38-61) of SARS-CoV-2 ORF6 protein, disrupting bidirectional transport between the nucleus and cytoplasm. Like Spike and NSP1-CTR, the ORF6-CTR is also disordered in nature but possesses gain of structure properties in minimal physiological conditions. As per studies, the residue such as Methionine at 58 th position in ORF6 is critical for interaction with Rae1-Nup98. Therefore, along with M58, we have identified a few other mutations from the literature and performed extensive structure modelling and dynamics studies using computational simulations. The exciting revelations in CTR models provide evidence of its structural flexibility and possible capabilities to perform multifunctionality inside the host.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Kumar, P., Saumya, K. U., Bhardwaj, T., & Giri, R.
- Affiliations
- Indian Institute of Technology Mandi (IN)
- Corresponding author
- Giri, Rajanish
- Venue
- Biophysical Chemistry
- Publisher
- openRxiv
- Published
- 2023-08-14
- Volume
- 318
- Pages
- 107384-107384
- ISSN
- 0301-4622 (ISSN-L)
- OpenAlex
- W4405679875
- Cited by
- 0
- References
- 1
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Biophysical Chemistry (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Department of Science and Technology, Ministry of Science and Technology, India (SPARC/2018-2019/P37/SL, BT/11/IYBA/2018/06, CRG/2019/005603)
- Indian Council of Medical Research (52/04/2020/BIO/BMS, 58/6/2020/PHA/BMS)
- Ministry of Education, India (CRG/2019/005603, SPARC/2018-2019/P37/SL, BT/11/IYBA/2018/06)
- Scheme for Promotion of Academic and Research Collaboration
- Science and Engineering Research Board (BT/11/IYBA/2018/06, CRG/2019/005603)
- 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
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 detection and testing
- Keywords
- C-terminal region, intrinsically disordered regions, protein structural dynamics, nuclear transport, protein structure modeling
- MeSH terms
- SARS-CoV-2, Humans, Methionine, Mutation, Protein Conformation, Viral Proteins, Amino Acid Motifs, Molecular Dynamics Simulation
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