1R0O

Crystal Structure of the Heterodimeric Ecdysone Receptor DNA-binding Complex

Summary for 1R0O

• Entry DOI: 10.2210/pdb1r0o/pdb
• Related: 1R0N
• Descriptor: Ecdysone Response Element, Ultraspiracle protein, Ecdysone receptor, ... (6 entities in total)
• Functional Keywords: ecdsyone receptor, ultraspiracle, nuclear receptor, dna binding domain, transcription-dna complex, transcription/dna
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Nucleus: P20153 P34021
• Total number of polymer chains: 4
• Total formula weight: 33904.24

Authors

Devarakonda, S.,Harp, J.M.,Kim, Y.,Ozyhar, A.,Rastinejad, F. (deposition date: 2003-09-22, release date: 2003-10-21, Last modification date: 2023-08-23)

Primary citation

Devarakonda, S.,Harp, J.M.,Kim, Y.,Ozyhar, A.,Rastinejad, F.
Structure of the Heterodimeric Ecdysone Receptor DNA-binding Complex
Embo J., 22:5827-5840, 2003

PubMed Abstract: Ecdysteroids initiate molting and metamorphosis in insects via a heterodimeric receptor consisting of the ecdysone receptor (EcR) and ultraspiracle (USP). The EcR-USP heterodimer preferentially mediates transcription through highly degenerate pseudo-palindromic response elements, resembling inverted repeats of 5'-AGGTCA-3' separated by 1 bp (IR-1). The requirement for a heterodimeric arrangement of EcR-USP subunits to bind to a symmetric DNA is unusual within the nuclear receptor superfamily. We describe the 2.24 A structure of the EcR-USP DNA-binding domain (DBD) heterodimer bound to an idealized IR-1 element. EcR and USP use similar surfaces, and rely on the deformed minor groove of the DNA to establish protein-protein contacts. As retinoid X receptor (RXR) is the mammalian homolog of USP, we also solved the 2.60 A crystal structure of the EcR-RXR DBD heterodimer on IR-1 and found the dimerization and DNA-binding interfaces to be the same as in the EcR-USP complex. Sequence alignments indicate that the EcR-RXR heterodimer is an important model for understanding how the FXR-RXR heterodimer binds to IR-1 sites.

PubMed: 14592980
DOI: 10.1093/emboj/cdg569

Experimental method

X-RAY DIFFRACTION (2.24 Å)