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283 RNA–protein interactions Kathleen B Hall Recent discoveries have revealed that there is a myriad of the binding affinity of any one RBD tends to be weak and, RNAs and associated RNA-binding proteins that spatially and at least in the case of hnRNP A1, the sequence specificity temporally appear in the cells of all organisms. The structures of of single domains might not be identical to that of the these RNA–protein complexes are providing valuable insights intact protein [2]. Many RBDs use the solvent-exposed into the binding modes and functional implications of these surface of the β sheet as an RNA-binding platform, but a interactions. Even the common RNA-binding domains (RBDs) surprising diversity in binding mechanisms is emerging. and the double stranded RNA binding motifs (dsRBMs) have been shown to exhibit a plethora of binding modes. Nucleolin In the nucleolus, nucleolin is thought to be required for the Addresses correct folding and packaging of pre-rRNA. These functions Department of Biochemistry and Molecular Biophysics, Box 8231, are mediated through the direct binding of nucleolin to two Washington University School of Medicine, 660 South Euclid Avenue, mutually exclusive RNA sequences [3]. The central domain St Louis, MO 63110, USA; e-mail: hall@bionmr3.wustl.edu of nucleolin contains four RBDs. RBD1 and RBD2, together Current Opinion in Structural Biology 2002, 12:283–288 with their 12 amino acid linker, form the binding site for the