Supplementary Figure 1: The unique topologies of the CCCH ZnF clusters of Unkempt.
From: Recognition of distinct RNA motifs by the clustered CCCH zinc fingers of neuronal protein Unkempt
(a) Disorder probability profile of the full-length mouse Unkempt protein determined by the DISOPRED prediction method within the PSIPRED protein sequence analysis workbench (http://bioinf.cs.ucl.ac.uk/psipred/). (b) Structure-based sequence alignment of ZnF1–3 and ZnF4–6 tandem ZnF cassettes. Zn-coordinating cysteine and histidine residues are highlighted in blue and the secondary structure elements are shown above the sequences. Residues involved in base stacking and hydrophobic interactions with RNA nucleotides are indicated by rectangles, while asterisks and triangles indicate residues that form hydrogen bonds (H bonds) with RNA bases via their backbone functional groups and side chains, respectively. The α, β and η symbols refer to α-helix, β-strands and 310-helix, respectively. Helices are displayed as squiggles, β-strands are rendered as arrows, strict β-turns as TT letters. (c) Superimposition of the ZnF4–6 cluster of Unkempt (light blue) and the CCCH ZnFs 5–7 of yeast Nab2 protein (red) revealing substantial differences in their topologies. (d) Comparison of ZnF1–3 of Unkempt (yellow) with the CCCH ZnFs 5–7 of yeast Nab2 protein (red) indicates structural diversity of both folds. Both comparisons were done by superimposing the most C-terminal ZnFs in each pair of clusters, i.e. ZnF3 and ZnF6 of Unkempt and ZnF7 of Nab2 protein.
