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Article

Two conserved oligomer interfaces of NSP7 and NSP8 underpin the dynamic assembly of SARS-CoV-2 RdRP.

Nucleic acids research - 4 Jun 2021

Biswal Mahamaya, Diggs Stephen, Xu Duo, Khudaverdyan Nelli, Lu Jiuwei, Fang Jian, Blaha Gregor, Hai Rong, Song Jikui

Abstract excerpt

Replication of the ∼30 kb-long coronavirus genome is mediated by a complex of non-structural proteins (NSP), in which NSP7 and NSP8 play a critical role in regulating the RNA-dependent RNA polymerase (RdRP) activity of NSP12. The assembly of NSP7, NSP8 and NSP12 proteins is highly dynamic in solution, yet the underlying mechanism remains elusive. We report the crystal structure of the complex between NSP7 and...

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Identifiers

PMID: 33999154
DOI: 10.1093/nar/gkab370
PMCID: PMC8191759

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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