SARS-CoV-2 Nidoviral RNA Uridylate‐Specific Endoribonuclease (NSP15); A Target Enabling Package
Creators
- 1. Physics Institute of Sao Carlos, University of Sao Paulo, Av. Joao Dagnone, 1100, Jardim Santa Angelina, São Carlos 13563-120, Brazil
- 2. Centre for Medicines Discovery, Old Road Campus Research Building, University of Oxford, Roosevelt Dr, Headington, Oxford OX3 7DQ
- 3. Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, OX11 0QX, United Kingdom
Description
The non-structural protein 15 (NSP15, NendoUSARS-CoV-2) from severe acute respiratory syndrome 2 virus (SARS-CoV-2) is an uridylate-specific endoribonuclease, likely responsible in the viral immune evasion mechanism. This TEP provides a set of reagents for further interrogation of the molecular function of NSP15. We have established a purification protocol for the active protein for biochemical and structural studies. Moreover, we have crystallised the protein and performed a crystallographic fragment screen which yielded several hits. Data generated here will be used for the development of enzyme inhibitors that would illuminate the biological role of the gene product, and eventually point the way to new antiviral therapies.
Notes
Files
NSP15 TEP_v1.pdf
Files
(1.8 MB)
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Additional details
Related works
- Is part of
- https://www.cmd.ox.ac.uk/teps (URL)
Funding
- A UK Hub to Catalyse Open Target Discovery. 106169
- Wellcome Trust