3oa1
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Crystal structure of phosphoprotein/Protein P/Protein M1 residues 69-297 from Rabies virus reveals degradation to C-terminal domain only
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Structural highlights
FunctionPHOSP_RABVP 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). Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. | ||||||||||||||||||||
This page was last modified 10:33, 21 February 2024.