7C20
Crystal structure of Rabies virus (Nishigahara strain) phosphoprotein C-terminal domain (K214A)
Summary for 7C20
| Entry DOI | 10.2210/pdb7c20/pdb |
| Descriptor | Phosphoprotein (1 entity in total) |
| Functional Keywords | phosphoprotein, viral protein |
| Biological source | Rabies virus (strain Nishigahara RCEH) (RABV) |
| Total number of polymer chains | 1 |
| Total formula weight | 12976.77 |
| Authors | Nomai, T.,Maenaka, K.,Ose, T. (deposition date: 2020-05-06, release date: 2021-03-17, Last modification date: 2023-11-29) |
| Primary citation | Sugiyama, A.,Nomai, T.,Jiang, X.,Minami, M.,Yao, M.,Maenaka, K.,Ito, N.,Gooley, P.R.,Moseley, G.W.,Ose, T. Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins. Biochem.Biophys.Res.Commun., 529:507-512, 2020 Cited by PubMed Abstract: Lyssavirus P protein is a multifunctional protein that interacts with numerous host-cell proteins. The C-terminal domain (CTD) of P is important for inhibition of JAK-STAT signaling enabling the virus to evade host immunity. Several regions on the surface of rabies virus P are reported to interact with host factors. Among them, an extended, discrete hydrophobic patch of P CTD is notable. Although structures of P CTD of two strains of rabies virus, and of mokola virus have been solved, the structure of P CTD for Duvenhage virus, which is functionally divergent from these species for immune evasion function, is not known. Here, we analyze the structures of P CTD of Duvenhage and of a distinct rabies virus strain to gain further insight on the nature and potential function of the hydrophobic surface. Molecular contacts in crystals suggest that the hydrophobic patch is important to intermolecular interactions with other proteins, which differ between the lyssavirus species. PubMed: 32703459DOI: 10.1016/j.bbrc.2020.05.195 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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