2XHS

Crystal structure of the ligand binding domain of Fushi tarazu factor 1 of Drosophila melanogaster.

Replaces:  2IZ2

Summary for 2XHS

• Entry DOI: 10.2210/pdb2xhs/pdb
• Related: 1FTZ 2IZ2
• Descriptor: NUCLEAR HORMONE RECEPTOR FTZ-F1, SEGMENTATION PROTEIN FUSHI TARAZU (3 entities in total)
• Functional Keywords: transcription
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY); More
• Total number of polymer chains: 2
• Total formula weight: 29793.49

Authors

Yoo, J.H.,Cho, H.S. (deposition date: 2010-06-21, release date: 2011-07-20, Last modification date: 2024-11-13)

Primary citation

Yoo, J.,Ko, S.,Kim, H.,Sampson, H.,Yun, J.H.,Choe, K.M.,Chang, I.,Arrowsmith, C.H.,Krause, H.M.,Cho, H.S.,Lee, W.
Crystal Structure of Fushi Tarazu Factor 1 Ligand Binding Domain/Fushi Tarazu Peptide Complex Identifies New Class of Nuclear Receptors.
J.Biol.Chem., 286:31225-, 2011

PubMed Abstract: The 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.

PubMed: 21775434
DOI: 10.1074/JBC.M111.252916

Experimental method

X-RAY DIFFRACTION (2.8 Å)