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

David S. Libich
, Antoine Baudin

Producción científica: Comment/debate › revisión exhaustiva

1 Cita (Scopus)

Resumen

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.

Idioma original	English (US)
Páginas (desde-hasta)	121-122
Número de páginas	2
Publicación	Structure
Volumen	31
N.º	2
DOI	https://doi.org/10.1016/j.str.2023.01.004
Estado	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

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