7c20 | pdb_00007c20

Crystal structure of Rabies virus (Nishigahara strain) phosphoprotein C-terminal domain (K214A)

spinqualitylabelsall models 7c20, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7c20 is a 1 chain structure with sequence from Rabies virus Nishigahara RCEH. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHOSP_RABVN Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body (By similarity). Publication Abstract from PubMed 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. Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins.,Sugiyama A, Nomai T, Jiang X, Minami M, Yao M, Maenaka K, Ito N, Gooley PR, Moseley GW, Ose T Biochem Biophys Res Commun. 2020 Aug 20;529(2):507-512. doi:, 10.1016/j.bbrc.2020.05.195. Epub 2020 Jul 2. PMID:32703459 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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