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

abstract

• 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.

authors

• Ivanov, Ivan

published proceedings

• J Virol

author list (cited authors)

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

citation count

• 71

complete list of authors

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

publication date

• April 2010

publisher

• American Society for Microbiology  Publisher

keywords

• Dimerization
• Phosphoproteins
• Protein Multimerization
• Protein Structure, Secondary
• Rabies Virus
• Sendai Virus
• Vesicular Stomatitis Indiana Virus
• Viral Proteins

Digital Object Identifier (DOI)

• 10.1128/JVI.02557-09

start page

• 3707

end page

• 3710

volume

• 84

issue

• 7

URL

• http://dx.doi.org/10.1128/jvi.02557-09

user-defined tag

• 3 Good Health and Well-Being