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. Author manuscript; available in PMC: 2015 Apr 3.
Published in final edited form as: J Mol Biol. 2013 Dec 12;426(7):1390–1406. doi: 10.1016/j.jmb.2013.11.031

Fig. 3. Structural ensembles of free and bound ETV6 are similar except for the unfolding of helix H5.

Fig. 3

The NMR-derived structural ensembles of (A) the ETV6D446–DNAsp complex (ETS domain helices and strands, red; CID helix H4, cyan) and (B) uninhibited ETV6R426 align closely to the lowest energy structure of inhibited ETV6R458 (green).16 CID helix H5, which blocks the DNA-binding interface of ETV6R458, is absent in ETV6R426 and unfolded in the ETV6D446-DNAsp complex. Although present in the latter complex, DNAsp was not included in the structure calculations. The N-terminal Gly-Ser-His-Met and unstructured residues (329-335 and 444-446) are not shown for clarity. Arrows point to the DNA-binding interface along helix H3.