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A key step in the activation of interferon‐inducible antiviral kinase PKR involves differential binding of viral double‐stranded RNA (dsRNA) to its two structurally similar N‐terminal dsRNA binding motifs, dsRBM1 and dsRBM2. We show here, using NMR spectroscopy, that dsRBM1 with higher RNA binding activity exhibits significant motional flexibility on a millisecond timescale as compared with dsRBM2 with lower RNA binding activity. We further show that dsRBM2, but not dsRBM1, specifically interacts with the C‐terminal kinase domain. These results suggest a dynamically tuned dsRNA binding mechanism for PKR activation, where motionally more flexible dsRBM1 anchors to dsRNA, thereby inducing a cooperative RNA binding for dsRBM2 to expose the kinase domain.
The EMBO Journal – Wiley
Published: Apr 16, 2001
Keywords: ; ; ;
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