2'-5'-oligoadenylate synthase
| 2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | OAS1_C | ||||||||
| Pfam | PF10421 | ||||||||
| InterPro | IPR018952 | ||||||||
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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]
References
- ^ Ghosh SK, Kusari J, Bandyopadhyay SK, Samanta H, Kumar R, Sen GC (1991). "Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships". J. Biol. Chem. 266 (23): 15293–9. PMID 1651324.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Hartmann R, Justesen J, Sarkar SN, Sen GC, Yee VC (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.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link)