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Details on Person When bound to viral double-stranded RNA (dsRNA), cytosolic 2...
| Class:Id | Summation:9012240 |
|---|---|
| _displayName | When bound to viral double-stranded RNA (dsRNA), cytosolic 2... |
| _timestamp | 2026-03-26 20:59:16 |
| created | [InstanceEdit:9012242] Shamovsky, Veronica, 2017-07-12 |
| literatureReference | [LiteratureReference:9012230] OAS proteins and cGAS: unifying concepts in sensing and responding to cytosolic nucleic acids [LiteratureReference:9012236] The Activation Mechanism of 2'-5'-Oligoadenylate Synthetase Gives New Insights Into OAS/cGAS Triggers of Innate Immunity [LiteratureReference:9012235] Viral encounters with 2',5'-oligoadenylate synthetase and RNase L during the interferon antiviral response [LiteratureReference:8983650] Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1 [LiteratureReference:9985938] Enzyme assays for synthesis and degradation of 2-5As and other 2'-5' oligonucleotides [LiteratureReference:9716358] Rapid RNase L-driven arrest of protein synthesis in the dsRNA response without degradation of translation machinery |
| modified | [InstanceEdit:9015149] Shamovsky, Veronica, 2017-08-08 [InstanceEdit:9614459] Shamovsky, Veronica, 2018-07-27 [InstanceEdit:9615278] Shamovsky, Veronica, 2018-07-31 [InstanceEdit:9986179] Shamovsky, Veronica, 2026-03-26 |
| text | When bound to viral double-stranded RNA (dsRNA), cytosolic 2′-5′-oligoadenylate synthetase 1 (OAS1) catalyzes the polymerization of ATP into 5′-triphosphorylated 2′-5′-linked oligoadenylates (2–5A). During this reaction, OAS1 transfers an AMP moiety from a donor ATP to the 2′-hydroxyl group of an acceptor substrate, which is either ATP or a preexisting 2–5A chain, forming dimers (ppp5′A(2′-5′)A) or extended oligomers (ppp5'A((2'-5')A)n), with pyrophosphate (PPi) released for each AMP residue added (Lohofener J et al., 2015; Poulsen JB et al., 2015). Structural studies show that dsRNA engagement induces an allosteric rearrangement that stabilizes the ATP-binding cleft by repositioning catalytic residues D75, D77, and D148 to coordinate two Mg²⁺ ions and facilitate ATP binding (Donovan J et al., 2013). This conformational change effectively couples dsRNA recognition to OAS1 enzymatic activation. The resulting 2–5A molecules act as second messengers that bind and activate latent RNase L, promoting its dimerization and triggering degradation of viral and cellular single-stranded RNA, thereby inducing translation arrest and inhibition of viral replication (Donovan J et al., 2017; reviewed by Silverman RH, 2007; Hornung V et al., 2014). |
| (summation) | [Polymerisation:8983680] OAS1 produces oligoadenylates [Homo sapiens] |
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