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Updated: Jun 16, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Structure of the dimerization domain of the rabies virus phosphoprotein
Ivan Ivanov1, Thibaut Crépin, Marc Jamin
1UVHCI, UMI 3265 UJF-EMBL-CNRS, BP 181, 38042 Grenoble, Cedex 9, France.
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.
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