ArticleJournal of biomolecular structure & dynamics2026
K294E change in the rotavirus factory forming protein NSP2 stabilizes a rare C-terminal conformation.
Article in Journal of biomolecular structure & dynamics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Rotaviruses (RVs) induce the formation of cytoplasmic viral factories, termed viroplasms, which are the sites of early particle assembly and viral RNA synthesis. The RV octameric nonstructural protein 2 (NSP2) plays critical, albeit incompletely understood, roles during viroplasm biogenesis. Previous work by our lab demonstrated that a RV bearing a lysine-to-glutamic acid (K294E) change in the flexible C-terminus of NSP2 exhibits defects in viral replication and induces smaller, more numerous viroplasms as compared to the wildtype (WT) virus. In this study, we sought to better understand if/how this K294E amino acid change altered the structure and/or dynamics of the NSP2 protein. We first determined the X-ray crystal structures of untagged, recombinant NSP2
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