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Human oligoadenylate synthetase 1 (OAS1) recognizes doubl...

Class:IdSummation:9977690
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Human oligoadenylate synthetase 1 (OAS1) recognizes doubl...

_timestamp2026-01-21 15:18:24
created[InstanceEdit:9977687] Orlic-Milacic, Marija, 2025-12-22
literatureReference[LiteratureReference:8983650] Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1
[LiteratureReference:9614441] pppA2'p5'A2'p5'A: an inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells
[LiteratureReference:9977696] Rotavirus Controls Activation of the 2'-5'-Oligoadenylate Synthetase/RNase L Pathway Using at Least Two Distinct Mechanisms
modified[InstanceEdit:9977708] Orlic-Milacic, Marija, 2025-12-22
[InstanceEdit:9977709] Orlic-Milacic, Marija, 2025-12-22
[InstanceEdit:9979785] Orlic-Milacic, Marija, 2026-01-21
text

Human oligoadenylate synthetase 1 (OAS1) recognizes double-stranded RNA (dsRNA) typically produced by viral infections. The X-ray crystal structure of human OAS1 bound to a model 18-bp dsRNA duplex revealed that dsRNA binding allosterically drives a functionally essential structural reorganization within human OAS1 that narrows the adenosine triphosphate (ATP)-binding cleft and repositions a catalytic residue to complete its active site (Donovan et al. 2013). Once stimulated by dsRNA, OAS1 uses ATP to synthesize a series of 5'-triphosphorylated 2'-5'-linked oligoadenylates containing two to more than five adenylyl residues. The 5'-triphosphorylated 2'-5’-linked triadenylate (i.e., ppp5’A2’p5’A2’p5’A) is typically the most abundant active species (Kerr and Brown 1978).

Rotavirus A (RV-A) dsRNAs, most likely genomic dsRNAs, are recognized by OAS. Knockdown of OAS1 significantly increases infectivity of the simian RV-A strain RRV in monkey kidney cell line MA104, while knockdown of OAS3 has no effect (Sánchez-Tacuba et al. 2015).

(summation)[BlackBoxEvent:9977691] RV-A dsRNA is an OAS1 ligand [Homo sapiens]
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Human oligoadenylate synthetase 1 (OAS1) recognizes doubl... (9977690)