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FIGURE 4:. Comparison between class A and class B Survivin paralogues. (A) Evolutionary relationships between Survivin proteins. The cladogram of Survivin protein based on sequence alignment in B. The evolution history was deduced using the minimum evolution method. The cladogram is drawn to scale, with branch lengths in the same units as those of the evolutionary distances used to infer the cladogram. Numbers show bootstrap values at the nodes. (B) Sequence alignment of Survivin BIR domains from selected organisms. Residues involved in zinc finger motif formation are marked in yellow. Residues H and R, which distinguish class A and B Survivin, are marked in red. Progressive dark shading indicates identity between 80 and 100%. Numbers on the left side of the alignment indicate the residue from which the alignment begins; numbers on the right are the last residues taken into alignment. Numbers in parentheses are the number of amino acids present in insertions that were removed from alignment. Numbers above the alignment indicate the residue numbering in hSurvivin. Letters from A to D mark helices, and black arrows numbered from 1 to 3 mark β-strands. Residues that form hydrogen bonds with H3 peptide are marked by blue rectangles. N-terminal and C-terminal variable regions and insertions were removed from alignment for clarity. (C) Superposition of the crystal structure of wild-type hSurvivin (gray) and homology model of xSurvivin-B (green carbon atoms). Mutated residues in Survivin (human H80 and Xenopus R89) and histone H3T3ph(1-4) residues are marked. Green dashes depict probable hydrogen bonds between the homology model of xSurvivin-B and H3T3ph(1-4) peptide.

Image published in: Niedzialkowska E et al. (2012)

© 2012 Niedzialkowska et al. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike license

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