SARS-CoV-2 Nsp8 N-terminal domain folds autonomously and binds dsRNA.
Nucleic Acids Res
; 51(18): 10041-10048, 2023 10 13.
Article
en En
| MEDLINE
| ID: mdl-37665006
ABSTRACT
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
SARS-CoV-2
Límite:
Humans
Idioma:
En
Revista:
Nucleic Acids Res
Año:
2023
Tipo del documento:
Article
País de afiliación:
España