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Literature DB >> 20089657

Structure of the dimerization domain of the rabies virus phosphoprotein.

Ivan Ivanov¹, Thibaut Crépin, Marc Jamin, Rob W H Ruigrok.

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.

Entities: Disease Species

Mesh：

Substances：

Year: 2010 PMID： 20089657 PMCID： PMC2838143 DOI： 10.1128/JVI.02557-09

Source DB: PubMed Journal: J Virol ISSN： 0022-538X Impact factor: 5.103

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