Hendra virus (HeV) is a 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 viral phosphoprotein (P) gene, which also encodes the V and W proteins as distinct products. V modulates the host response to infection by targeting numerous host proteins. Here, by combining in vitro and in vivo analyses, we show nuclear transport 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.