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. 2013 Jan 24;450(Pt 1):85–94. doi: 10.1042/BJ20121382

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© 2013 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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(A) Structural comparisons of RBM25 PWI with the SRm160 and Prp3 PWI domains. Only our structure shows the structure of the flanking basic region. H1 and H4 are shown in green, H2 and H3 are shown in red, the N-elements (HN) are shown in yellow, the C-element (HC) is shown in wheat, and the flanking basic region is shown in orange. (B) Comparison of surface electrostatic potentials of RBM25 PWI domain with the SRm160 and Prp3 PWI domains. The red broken box encloses the flanking basic region. (C) The highly conserved phenylalanine residue in H4 packs against the tryptophan and isoleucine residues in the highly conserved signature Pro-Trp-Ile sequence of H1. Single-letter code is used for amino acids.