InterPro domain: IPR014720

In contrast to other RNA-binding domains, the about 65 amino acids long dsRBD domain [ 1 , 2 , 3 ] has been found in a number of proteins that specifically recognise double-stranded RNAs. The dsRBD domain is also known as DSRM (Double-Stranded RNA-binding Motif). dsRBD proteins are mainly involved in posttranscriptional gene regulation, for example by preventing the expression of proteins or by mediating RNAs localization. This domain is also found in RNA editing proteins. Interaction of the dsRBD with RNA is unlikely to involve the recognition of specific sequences [ 4 , 5 , 6 ]. Nevertheless, multiple dsRBDs may be able to act in combination to recognise the secondary structure of specific RNAs (i.e. Staufen) [ 7 ]. NMR analysis of the third dsRBD of Drosophila Staufen have revealed an alpha-beta-beta-beta-alpha structure [ 7 ].

1. A conserved double-stranded RNA-binding domain. Proc. Natl. Acad. Sci. U.S.A. 89, 10979-83
2. Conserved structures and diversity of functions of RNA-binding proteins. Science 265, 615-21
3. Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enzyme for nuclear RNA editing. Proc. Natl. Acad. Sci. U.S.A. 91, 11457-61
4. Interactions between double-stranded RNA regulators and the protein kinase DAI. Mol. Cell. Biol. 12, 5238-48
5. Preferential selection of adenosines for modification by double-stranded RNA adenosine deaminase. EMBO J. 13, 5701-11
6. Structural characterization of a ribonuclease III processing signal. Nucleic Acids Res. 22, 604-12
7. NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J. 14, 3563-71