OAS3 binds viral dsRNA

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Influenza A virus, Sindbis virus, Dengue virus, West Nile virus
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Viral dsRNA-activated oligoadenylate synthetase 3 (OAS3) exhibits a strong preference for long dsRNA. A study that included the crystal structure of the N-terminal enzymatically inactive 2'-5' oligoadenylate synthetase domain of human OAS3 (hOAS3.DI) in complex with 19-bp dsRNA indicated that this domain I (DI) subunit has high affinity for the binding of long (>50 bp) dsRNA, which then is presented to the enzymatically active C-terminal domain III (DIII) of OAS3 that produces 5’-triphosphorylated 2'-5' olgoadenylates from ATP (Donovan J et al. 2015). OAS3 was reported to be the major antiviral human OAS isoform (Li Y et al. 2016).
Literature References
PubMed ID Title Journal Year
25775560 Structural mechanism of sensing long dsRNA via a noncatalytic domain in human oligoadenylate synthetase 3

Korennykh, A, Rath, S, Whitney, G, Donovan, J

Proc. Natl. Acad. Sci. U.S.A. 2015
26858407 Activation of RNase L is dependent on OAS3 expression during infection with diverse human viruses

Silverman, RH, Dong, B, Wang, Y, Weiss, SR, Banerjee, S, Gaughan, C, Goldstein, SA, Li, Y

Proc. Natl. Acad. Sci. U.S.A. 2016
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