Structure of the dimerization domain of the rabies virus phosphoprotein.
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.
Ivanov
Ivan
I
UVHCI, UMI 3265 UJF-EMBL-CNRS, BP 181, 38042 Grenoble, Cedex 9, France.
Crépin
Thibaut
T
Jamin
Marc
M
Ruigrok
Rob W H
RW
D019281:Dimerization; D010750:Phosphoproteins / Q000737:chemistry*; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D011820:Rabies virus / Q000737:chemistry*; D029082:Sendai virus / Q000737:chemistry; D014721:Vesicular stomatitis Indiana virus / Q000737:chemistry; D014764:Viral Proteins / Q000737:chemistry*
D010750:Phosphoproteins; D014764:Viral Proteins