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. 2011 Jul 20;286(36):31225–31231. doi: 10.1074/jbc.M111.252916

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — The novel LBP of the LBD of FTZ-F1. A, ribbon representations of the LBP of FTZ-F1 in two different views are displayed with H6 in cyan and with β-strands in white. B, detailed intramolecular interactions between residues of LBP (yellow) and H6 (cyan) are shown. C, activity assay of wild-type and mutant proteins of FTZ-F1 found H6 was essential for the transcriptional activity of FTZ-F1 because mutants of H6 significantly reduced transcriptional activity compared with wild type. Triple, L901D, L904D, and L9006D; Quadruple, 901D, L904D, L906D, and L912D; G6, 12 residues from approximately Leu-901–Leu-912 were replaced with six glycines.