9zrd
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Crystal structure of macrodomain from Eastern Equine Encephalitis Virus in complex with Adenosine diphosphate ribose
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Structural highlights
FunctionQ66580_EEEV Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.[ARBA:ARBA00002589] Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis. Displays mono-ADP-ribosylhydrolase activity. ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication. Binds proteins of FXR and G3BP families and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs. The nsp3-FXR and nsp3-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP and FXR family members to self-assemble and bind DNA.[ARBA:ARBA00053052] Contents | ||||||||||||||||||||
This page was last modified 05:13, 13 August 2026.