Piece of the puzzle: Remdesivir disassembles the multimeric SARS-CoV-2 RNA-dependent RNA polymerase complex.

ABSTRACT: The recently emerged SARS-like coronavirus (SARS-CoV-2) has continued to spread rapidly among humans with alarming upsurges in global mortality rates. A major key to tackling this virus is to disrupt its RNA replication process as previously reported for Remdesivir (Rem-P₃). In this study, we theorize, using computational simulations, novel mechanisms that may underlie the binding of Rem-P₃ to SARS-CoV-2 RdRp-NSPs complex; a multimeric assembly that drives viral RNA replication in human hosts. Findings revealed that while ATP-binding stabilized the replicative tripartite, Rem-P₃ disintegrated the RdRp-NSP complex, starting with the detachment of the NSP7-NSP8 heterodimer followed by minimal displacement of the second NSP8 subunit (NSP8_II). More s

SUBMITTER: Olotu FA 

PROVIDER: S-EPMC8014903 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature