Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of the dimerization domain of the rabies virus phosphoprotein.,Ivanov I, Crepin T, Jamin M, Ruigrok RW J Virol. 2010 Apr;84(7):3707-10. Epub 2010 Jan 20. PMID:20089657[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ivanov I, Crepin T, Jamin M, Ruigrok RW. Structure of the dimerization domain of the rabies virus phosphoprotein. J Virol. 2010 Apr;84(7):3707-10. Epub 2010 Jan 20. PMID:20089657 doi:10.1128/JVI.02557-09
