2'-5'-oligoadenylate synthase
In molecular biology, 2'-5'-oligoadenylate synthetase is an enzyme 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 (RNASEL), resulting in degradation of viral RNA and inhibition of virus replication.[1]
2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus | |||||||||
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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 (between what?) at the extreme C-terminal end.[2]
See also
References
- 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.
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