In molecular biology, 2'-5'-oligoadenylate synthetase (2-5A synthetase) is an enzyme (EC 2.7.7.84) that reacts to interferon signal. It is an antiviral enzyme that counteracts viral attack by degrading RNAs, both viral and host. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'-5'-oligoadenylates, which activate latent ribonuclease (RNase-L), resulting in degradation of viral RNA and inhibition of virus replication.[1]
2'-5'-oligoadenylate synthetase | |||||||||
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Identifiers | |||||||||
Symbol | OAS1_C | ||||||||
Pfam | PF10421 | ||||||||
InterPro | IPR018952 | ||||||||
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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[clarification needed] at the extreme C-terminal end.[2]
Human proteins
editSee also
editReferences
edit- ^ 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.
- ^ 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.