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• W1972683642 abstract "Significance Double-stranded RNA (dsRNA) is a pathogen-associated molecular pattern that triggers the type-I interferon (IFN) response in mammalian cells. The IFN response up-regulates several dsRNA sensors, including closely related oligoadenylate synthetases (OAS). The functional roles of different oligoadenylate synthetases in dsRNA surveillance are not understood. Here, we use X-ray crystallography and biochemistry to demonstrate that human OAS1 and OAS3 recognize dsRNA molecules of different length. We show that domain duplication accompanied by a loss of catalytic activity provides the mechanism for sensing long dsRNA by OAS3. Our studies thus reveal different functions of OAS1 and OAS3 in dsRNA surveillance, identify a key role of domain duplication in the OAS family, and advance the fundamental understanding of the human innate immune system." @default.
• W1972683642 created "2016-06-24" @default.
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• W1972683642 date "2015-03-16" @default.
• W1972683642 modified "2023-10-17" @default.
• W1972683642 title "Structural mechanism of sensing long dsRNA via a noncatalytic domain in human oligoadenylate synthetase 3" @default.
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• W1972683642 doi "https://doi.org/10.1073/pnas.1419409112" @default.
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