Conformational ensemble of the NSP1 CTD in SARS-CoV-2: Perspectives from the free energy landscape.

ABSTRACT: The nonstructural protein-1 (NSP1) of the severe acute respiratory syndrome-associated coronavirus 2 plays a crucial role in the translational shutdown and immune evasion inside host cells. Despite its known intrinsic disorder, the C-terminal domain (CTD) of NSP1 has been reported to form a double α-helical structure and block the 40S-ribosomal channel for mRNA translation. Experimental studies indicate that NSP1 CTD functions independently from the globular N-terminal region separated with a long linker domain, underscoring the necessity of exploring the standalone conformational ensemble. In this contribution, we utilize exascale computing resources to yield unbiased molecular dynamics simulation of NSP1 CTD in all-atom resolution starting from multiple initial seed structures. A data-dr

SUBMITTER: Dutta P 

PROVIDER: S-EPMC9928668 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature