Structure of the dimerization domain of the rabies virus phosphoprotein. Academic Article uri icon


  • The crystal structure of the dimerization domain of rabies virus phosphoprotein was determined. The monomer consists of two alpha-helices that make a helical hairpin held together mainly by hydrophobic interactions. The monomer has a hydrophilic and a hydrophobic face, and in the dimer two monomers pack together through their hydrophobic surfaces. This structure is very different from the dimerization domain of the vesicular stomatitis virus phosphoprotein and also from the tetramerization domain of the Sendai virus phosphoprotein, suggesting that oligomerization is conserved but not structure.

published proceedings

  • J Virol

author list (cited authors)

  • Ivanov, I., Crpin, T., Jamin, M., & Ruigrok, R.

citation count

  • 65

complete list of authors

  • Ivanov, Ivan||Crépin, Thibaut||Jamin, Marc||Ruigrok, Rob WH

publication date

  • April 2010