Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide (FTZPEP) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, FTZPEP formed α-helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of FTZPEP. The solution structure of FTZPEP in the presence of FTZ-F1 displays a long stretch of the α-helix with a bend in the middle of helix.
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