Order and disorder bound together in SARS-CoV-2 Nsp1 suppress host translation

David S. Libich; Antoine Baudin

doi:10.1016/j.str.2023.01.004

Order and disorder bound together in SARS-CoV-2 Nsp1 suppress host translation

Research output: Contribution to journal › Comment/debate › peer-review

Abstract

In this issue of Structure, Wang et al. investigate the interplay between folded and disordered regions of the SARS-CoV-2 non-structural protein 1 (Nsp1) that promotes the suppression of host protein translation. Their investigation will lead to novel avenues to therapeutically target critical viral functions necessary for host immune-response suppression.

Original language	English (US)
Pages (from-to)	121-122
Number of pages	2
Journal	Structure
Volume	31
Issue number	2
DOIs	https://doi.org/10.1016/j.str.2023.01.004
State	Published - Feb 2 2023

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.str.2023.01.004

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title = "Order and disorder bound together in SARS-CoV-2 Nsp1 suppress host translation",

abstract = "In this issue of Structure, Wang et al. investigate the interplay between folded and disordered regions of the SARS-CoV-2 non-structural protein 1 (Nsp1) that promotes the suppression of host protein translation. Their investigation will lead to novel avenues to therapeutically target critical viral functions necessary for host immune-response suppression.",

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AB - In this issue of Structure, Wang et al. investigate the interplay between folded and disordered regions of the SARS-CoV-2 non-structural protein 1 (Nsp1) that promotes the suppression of host protein translation. Their investigation will lead to novel avenues to therapeutically target critical viral functions necessary for host immune-response suppression.

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Order and disorder bound together in SARS-CoV-2 Nsp1 suppress host translation

Abstract

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