2'-5'-oligoadenylate synthase

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2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus
Symbol OAS1_C
Pfam PF10421
InterPro IPR018952

In molecular biology, 2'-5'-oligoadenylate synthetase is an enzyme. It is an antiviral enzyme that counteracts viral attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'-5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication.[1]

The C-terminal half of 2'-5'-oligoadenylate synthetase, also referred to as domain 2 of the enzyme, is largely alpha-helical and homologous to a tandem ubiquitin repeat. It carries the region of enzymatic activity between at the extreme C-terminal end.[2]


  1. ^ Ghosh SK, Kusari J, Bandyopadhyay SK, Samanta H, Kumar R, Sen GC (August 1991). "Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships". J. Biol. Chem. 266 (23): 15293–9. PMID 1651324. 
  2. ^ Hartmann R, Justesen J, Sarkar SN, Sen GC, Yee VC (November 2003). "Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase". Mol. Cell 12 (5): 1173–85. doi:10.1016/S1097-2765(03)00433-7. PMID 14636576. 

This article incorporates text from the public domain Pfam and InterPro IPR018952