SARS-CoV-2 Nsp8 N-terminal domain folds autonomously and binds dsRNA.

Publication date: Sep 04, 2023

The SARS-CoV-2 Nsp8 protein is a critical component of the RNA replicase, as its N-terminal domain (NTD) anchors Nsp12, the RNA, and Nsp13. Whereas its C-terminal domain (CTD) structure is well resolved, there is an open debate regarding the conformation adopted by the NTD as it is predicted as disordered but found in a variety of complex-dependent conformations or missing from many other structures. Using NMR spectroscopy, we show that the SARS CoV-2 Nsp8 NTD features both well folded secondary structure and disordered segments. Our results suggest that while part of this domain corresponding to two long α-helices forms autonomously, the folding of other segments would require interaction with other replicase components. When isolated, the α-helix population progressively declines towards the C-termini but surprisingly binds dsRNA while preserving structural disorder.

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Concepts Keywords
Anchors Binds
Disorder Cov
Nsp12 Critical
Proteins Disordered
Spectroscopy Domain


Type Source Name
disease VO population
drug DRUGBANK Coenzyme M
disease MESH COVID 19 pandemic
pathway REACTOME Reproduction
drug DRUGBANK Tacrine
disease IDO production
drug DRUGBANK Thioredoxin
drug DRUGBANK Histidine
disease IDO site
drug DRUGBANK Isopropyl beta-D-thiogalactopyranoside
disease VO protocol
drug DRUGBANK Dextrose unspecified form
drug DRUGBANK Imidazole
drug DRUGBANK Flunarizine
drug DRUGBANK Sodium lauryl sulfate
drug DRUGBANK Pirenzepine
drug DRUGBANK Indoleacetic acid
disease IDO process
disease VO URE
drug DRUGBANK Esomeprazole
drug DRUGBANK Proline
drug DRUGBANK Pentaerythritol tetranitrate
drug DRUGBANK Ademetionine
drug DRUGBANK Gold
drug DRUGBANK Acetylcholine
disease IDO replication
drug DRUGBANK Erythropoietin
disease IDO facility
disease IDO cell
disease VO efficient
drug DRUGBANK Amber
disease MESH dissociation

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