Structural highlights
Publication Abstract from PubMedThe interaction between the orphan nuclear receptor FTZ-F1 (Fushi tarazu factor 1) and the segmentation gene protein FTZ is critical for specifying alternate parasegments in the Drosophila embryo. Here, we have determined the structure of the FTZ-F1 ligand-binding domain (LBD).FTZ peptide complex using x-ray crystallography. Strikingly, the ligand-binding pocket of the FTZ-F1 LBD is completely occupied by helix 6 (H6) of the receptor, whereas the cofactor FTZ binds the co-activator cleft site of the FTZ-F1 LBD. Our findings suggest that H6 is essential for transcriptional activity of FTZ-F1; this is further supported by data from mutagenesis and activity assays. These data suggest that FTZ-F1 might belong to a novel class of ligand-independent nuclear receptors. Our findings are intriguing given that the highly homologous human steroidogenic factor-1 and liver receptor homolog-1 LBDs exhibit sizable ligand-binding pockets occupied by putative ligand molecules. Crystal structure of fushi tarazu factor 1 ligand binding domain/fushi tarazu Peptide complex identifies new class of nuclear receptors.,Yoo J, Ko S, Kim H, Sampson H, Yun JH, Choe KM, Chang I, Arrowsmith CH, Krause HM, Cho HS, Lee W J Biol Chem. 2011 Sep 9;286(36):31225-31. Epub 2011 Jul 20. PMID:21775434[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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