3L32
Structure of the dimerisation domain of the rabies virus phosphoprotein
Summary for 3L32
| Entry DOI | 10.2210/pdb3l32/pdb |
| Descriptor | Phosphoprotein (2 entities in total) |
| Functional Keywords | antiparallel alpha-helices, viral protein, dimerisation domain, rabies virus, phosphoprotein |
| Biological source | Rabies virus |
| Cellular location | Phosphoprotein: Virion. Isoform P3: Host nucleus (By similarity). Isoform P4: Host nucleus (By similarity). Isoform P5: Host nucleus (By similarity): Q0GBY3 |
| Total number of polymer chains | 2 |
| Total formula weight | 10686.28 |
| Authors | Ivanov, I.,Crepin, T.,Jamin, M.,Ruigrok, R.W.H. (deposition date: 2009-12-16, release date: 2010-02-16, Last modification date: 2024-03-20) |
| Primary citation | Ivanov, I.,Crepin, T.,Jamin, M.,Ruigrok, R.W.H. Structure of the dimerisation domain of the rabies virus phosphoprotein J.Virol., 2010 Cited by PubMed 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. PubMed: 20089657DOI: 10.1128/JVI.02557-09 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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