A domain of all trades: The enzymatic versatility of the NiRAN domain

Adam Osinski; Vincent S. Tagliabracci

doi:10.1016/j.molcel.2023.10.009

A domain of all trades: The enzymatic versatility of the NiRAN domain

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

Abstract

The SARS-CoV-2 NiRAN domain is essential for viral replication. Despite adopting a pseudokinase fold, it catalyzes three distinct biochemical reactions from a single active site. In this issue of Molecular Cell, Small et al.¹ elucidate the structural intricacies of the NiRAN domain shedding light on the factors that underlie its remarkable versatility.

Original language	English (US)
Pages (from-to)	3758-3760
Number of pages	3
Journal	Molecular cell
Volume	83
Issue number	21
DOIs	https://doi.org/10.1016/j.molcel.2023.10.009
State	Published - Nov 2 2023

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2023.10.009

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title = "A domain of all trades: The enzymatic versatility of the NiRAN domain",

abstract = "The SARS-CoV-2 NiRAN domain is essential for viral replication. Despite adopting a pseudokinase fold, it catalyzes three distinct biochemical reactions from a single active site. In this issue of Molecular Cell, Small et al.1 elucidate the structural intricacies of the NiRAN domain shedding light on the factors that underlie its remarkable versatility.",

author = "Adam Osinski and Tagliabracci, {Vincent S.}",

note = "Publisher Copyright: {\textcopyright} 2023 Elsevier Inc.",

year = "2023",

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AU - Tagliabracci, Vincent S.

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AB - The SARS-CoV-2 NiRAN domain is essential for viral replication. Despite adopting a pseudokinase fold, it catalyzes three distinct biochemical reactions from a single active site. In this issue of Molecular Cell, Small et al.1 elucidate the structural intricacies of the NiRAN domain shedding light on the factors that underlie its remarkable versatility.

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JO - Molecular cell

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A domain of all trades: The enzymatic versatility of the NiRAN domain

Abstract

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