Hendra virus (HeV) is a highly pathogenic zoonotic paramyxovirus that causes severe disease and a high incidence of fatality in infected humans. Despite recurrent outbreaks and potential for human lethality, no vaccine or anti-viral agent is available to prevent or treat human HeV infection. Key to HeV pathogenicity is the co-transcriptional mRNA editing of the phosphoprotein (P) gene to generate additional mRNAs encoding the V and W proteins. The V protein modulates the host response to infection by targeting numerous host proteins. Here, by combining in vitro and in vivo analyses, we show both nuclear import and export receptors are amongst those targeted by HeV V, and play a role in infection. Structural analysis reveals HeV V is inherently disordered and gains structure upon binding its target nuclear transport receptors; a trait that offers numerous functional advantages. These findings broaden our understanding of HeV-host interactions.