Back

SARS-CoV-2 Nsp8 N-terminal domain dimerizes and harbors autonomously folded elements

Trevino, M. A.; Pantoja-Uceda, D.; Laurents, D. V.; Mompean, M.

2021-03-15 biophysics
10.1101/2021.03.12.435186 bioRxiv
Show 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 -helices forms autonomously, the folding of other segments would require interaction with other replicase components. When isolated, the -helix population progressively declines towards the C-termini, and dynamics measurements indicate that the Nsp8 NTD behaves as a dimer under our conditions.

Matching journals

The top 6 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.