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2'-5'-Oligoadenylate synthetase 1 (OAS1) is an interferon-induced enzyme that plays a key role in innate antiviral immunity. Upon binding viral double-stranded RNA, OAS1 catalyzes the synthesis of 2'-5'-linked oligoadenylates from ATP, which activate RNase L to cleave single-stranded RNA, thereby inhibiting viral replication and inducing apoptosis. OAS1 activity is determined by both sequence and structural features of the RNA ligand, and its function may be modulated by isoform diversity, genetic variation, and interaction with cellular proteins. Dysregulation of OAS1 is implicated in susceptibility to viral infections and may contribute to immune pathology under certain conditions[1][2][3].
Double-stranded RNA (dsRNA) binding leads to enzyme activation[2] Synthesizes 2'-5'-linked oligoadenylates (2-5A) from ATP 2-5A activates latent RNase L, resulting in RNA cleavage and inhibition of viral replication[2]
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