Rhabdovirus is a negative strand RNA virus that packages a ribonucleoprotein (RNP) complex. The RNP is composed of a genome that is encapsidated completely by the nucleoprotein (N). Structural comparisons of the RNA-nucleoprotein complexes from two members, vesicular stomatitis virus (VSV) and rabies virus (RABV), revealed highly conserved characteristics of folding, RNA binding, and assembly despite their lack of significant homology in amino acid sequence. The RNA binding cavity is located between two conserved domains formed by α-helices, but the positively charged residues that coordinate with the phosphate groups are at different sites. The intermolecular interactions among N molecules have a conserved pattern that is rendered, however, by different residues. The curvature of the RABV N-RNA complex in the crystal structure is larger than that of the VSV N-RNA complex. The more relaxed curvature allows the bases in the RNA to stack more tightly, and at the same time, the helices near the C-terminus move into the created space in order to cover the bound RNA. This may explain how the RNP can adopt different conformations from being packed as a superhelix in the virion to a relaxed linear structure once being delivered into the cytoplasm. © 2007 Elsevier B.V. All rights reserved.