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. 2011 Oct 14;31(1):162–174. doi: 10.1038/emboj.2011.367

Figure 1.

Figure 1

Solution structure of the SRSF2 RRM (aa 1–101) in the free state. (A) Schematic representation of the full-length SRSF2. The protein is shown with the amino-acid sequence of the RRM used in these studies. The β-strands are coloured in orange, α-helices in red and both conserved RNP motifs are underlined. Numbering is according to the PDB sequence. (B) Backbone traces (N, Cα and C′) of the 20 lowest energy structures of the free-state SRSF2 RRM (aa 1--101) superimposed on the backbone of the structured part (aa 10–93). Protein backbone of the RRM (aa 15–90) in grey, N-terminus (aa 1–14) in blue and C-terminus (aa 91–101) in dark green. (C) Ribbon structure of the free-state SRSF2 RRM. Characteristic residues are in stick representation, coloured green for carbon, red for oxygen and blue for nitrogen. (D) Close-up view on the hinge between β-strand 1 and the N-terminus with the same colour code than for (C) plus yellow for sulphur. Hydrogen bonds are presented as violet dashed lines. Figures (B–D) were generated with MOLMOL (Koradi et al, 1996).