The dimerization domain of SARS-CoV-2 nucleocapsid protein is partially disordered and forms a dynamic high-affinity dimer.

ABSTRACT: The SARS-CoV-2 nucleocapsid (N) drives the compaction and packaging of the viral genome. Here, we focused on quantifying the mechanisms that control dimer formation utilizing single-molecule Förster resonance energy transfer to investigate the conformations and energetics of the dimerization domain in the context of the full-length protein. Under monomeric conditions, we observed significantly expanded configurations of the dimerization domain (compared to the folded dimer structure), which is consistent with a dynamic conformational ensemble. The addition of unlabeled protein stabilizes a folded dimer configuration with a high mean transfer efficiency, which is in agreement with predictions based on known structures. Dimerization is characterized by a dissociation constant of ~12 nM at 23

SUBMITTER: Cubuk J 

PROVIDER: S-EPMC12385586 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature