Author: Rajanish Giri; Taniya Bhardwaj; Meenakshi Shegane; Bhuvaneshwari R. Gehi; Prateek Kumar; Kundlik Gadhave
Title: Dark Proteome of Newly Emerged SARS-CoV-2 in Comparison with Human and Bat Coronaviruses Document date: 2020_3_14
ID: n7ylgqfu_68
Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.13.990598 doi: bioRxiv preprint protein 1 (Nsp1) . This protein acts as a host translation inhibitor as it binds to the 40S subunit of the ribosome and blocks the translation of cap-dependent mRNAs as well as mRNAs that uses the internal ribosome entry site (IRES) [124] . Figure 19D shows the NMR solution structure (PDB ID: 2GDT) of Human.....
Document: The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.13.990598 doi: bioRxiv preprint protein 1 (Nsp1) . This protein acts as a host translation inhibitor as it binds to the 40S subunit of the ribosome and blocks the translation of cap-dependent mRNAs as well as mRNAs that uses the internal ribosome entry site (IRES) [124] . Figure 19D shows the NMR solution structure (PDB ID: 2GDT) of Human SARS nsp1 protein (13-128 residues), whereas residues 117-180 were not included in this structural analysis [125] .
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