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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.
Future versions of this TEP will contain experimental data from the NSP15 TEP.
Immunology, NSP15, Biophysics, Plant Biology, Target Enabling Package, Biochemistry, Virology, Drug Discovery, Chemical Biology, Genetics, Nidoviral RNA Uridylate‐Specific Endoribonuclease, Disease, Drug Target, Molecular Biology, Corona Virus, SARS-CoV-2, Protein, Structure Discovery, Structure, COVID-19, Probe, Mental Health, Infectious Diseases, Orphan disease, Structural Genomics, Biological Sciences not elsewhere classified
Immunology, NSP15, Biophysics, Plant Biology, Target Enabling Package, Biochemistry, Virology, Drug Discovery, Chemical Biology, Genetics, Nidoviral RNA Uridylate‐Specific Endoribonuclease, Disease, Drug Target, Molecular Biology, Corona Virus, SARS-CoV-2, Protein, Structure Discovery, Structure, COVID-19, Probe, Mental Health, Infectious Diseases, Orphan disease, Structural Genomics, Biological Sciences not elsewhere classified
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