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• W2029842408 endingPage "7513" @default.
• W2029842408 startingPage "7505" @default.
• W2029842408 abstract "Protein interactions with double-stranded RNA (dsRNA) are critical for many cell processes; however, in contrast to protein-dsDNA interactions, surprisingly little is known about the molecular basis of protein-dsRNA interactions. A large and diverse class of proteins that bind dsRNA do so by utilizing an approximately 70 amino acid motif referred to as the dsRNA-binding domain (dsRBD). We have determined a 1.9 A resolution crystal structure of the second dsRBD of Xenopus laevis RNA-binding protein A complexed with dsRNA. The structure shows that the protein spans 16 bp of dsRNA, interacting with two successive minor grooves and across the intervening major groove on one face of a primarily A-form RNA helix. The nature of these interactions explains dsRBD specificity for dsRNA (over ssRNA or dsDNA) and the apparent lack of sequence specificity. Interestingly, the dsRBD fold resembles a portion of the conserved core structure of a family of polynucleotidyl transferases that includes RuvC, MuA transposase, retroviral integrase and RNase H. Structural comparisons of the dsRBD-dsRNA complex and models proposed for polynucleotidyl transferase-nucleic acid complexes suggest that similarities in nucleic acid binding also exist between these families of proteins." @default.
• W2029842408 created "2016-06-24" @default.
• W2029842408 creator A5037384889 @default.
• W2029842408 creator A5082938118 @default.
• W2029842408 date "1998-12-15" @default.
• W2029842408 modified "2023-10-06" @default.
• W2029842408 title "Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA" @default.
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• W2029842408 doi "https://doi.org/10.1093/emboj/17.24.7505" @default.
• W2029842408 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1171094" @default.
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• W2029842408 hasPublicationYear "1998" @default.
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