OAS3 binds viral dsRNA

Stable Identifier
R-HSA-8985157
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Influenza A virus, Sindbis virus, Dengue virus, West Nile virus
Compartment
cytosol
ReviewStatus
5/5
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OAS3 binds viral dsRNA
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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

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

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

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

Proc. Natl. Acad. Sci. U.S.A. 2016
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Authored
Shamovsky, V  (2017-03-27)
Reviewed
D'Eustachio, P  (2017-12-02)
Silverman, RH  (2018-07-31)
Created
Shamovsky, V  (2017-04-12)
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