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. 2014 Oct 10;42(20):12885–12898. doi: 10.1093/nar/gku930

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© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Structure of yeast Prp28-ΔN and homology to Vasa. (A) A stereo view of the tertiary structure of the B protomer of Prp28-ΔN is shown as a cartoon model, with β strands colored magenta, α helices colored cyan and 3₁₀ helices colored blue. The N and C termini are indicated. AMPPNP bound to the N domain is depicted as a stick model. (B) The secondary structure elements of yeast Prp28 and Drosophila Vasa (colored as in panel A) are shown above and below their aligned amino acid sequences, with β strands rendered as arrows and helices as cylinders. Gaps in the alignment are indicated by dashes. Positions of amino acid side chain identity/similarity are indicated by • above the sequence. The conserved amino acids in Prp28 that were target for alanine scanning in Prp28 are highlighted in yellow boxes.