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Comment
. 2020 Oct 9;5(1):234.
doi: 10.1038/s41392-020-00350-0.

Inhibition of translation and immune responses by the virulence factor Nsp1 of SARS-CoV-2

Kendra R Vann  1 , Adam H Tencer  1 , Tatiana G Kutateladze  2
Affiliations
Comment

Inhibition of translation and immune responses by the virulence factor Nsp1 of SARS-CoV-2

Kendra R Vann et al. Signal Transduct Target Ther. .
No abstract available

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Conflict of interest statement

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1
Structural basis for binding of the SARS-CoV-2 Nsp1 protein to the ribosomal 40S subunit. a Domain architecture of the SARS-CoV-2 Nsp1 protein (top). The N-terminal domain (NTD) and the C-terminal α-helices are labeled and colored light blue and red, respectively. Cryo-EM structure of the Nsp1 protein bound to 40S (PDB 6zlw) (bottom). The two C-terminal α-helices of Nsp1 (red) insert into the mRNA entry channel of 40S (gray). The resolution of the NTD region of Nsp1 in the cryo-EM density map was insufficient to unambiguously identify this domain. b Close view of the interface of the 40S:Nsp1 complex (PDB 6zlw). The two C-terminal α-helices of Nsp1 (red) make contacts with ribosomal rRNA h18 (orange phosphate backbone and blue nucleotide bases) and with the ribosomal proteins uS3 (light blue) and uS5 (light green). The K164 and H165 residues of the KH motif of Nsp1 are shown as red sticks
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Comment on

References

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