Structure of the heterodimeric ecdysone receptor DNA-binding complex
AUTOR(ES)
Devarakonda, Srikripa
FONTE
Oxford University Press
RESUMO
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 Å 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 Å 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=275426Documentos Relacionados
- Heterodimeric DNA-binding dyes designed for energy transfer: stability and applications of the DNA complexes.
- Heterodimeric DNA-binding dyes designed for energy transfer: synthesis and spectroscopic properties.
- Structure of the RXR–RAR DNA-binding complex on the retinoic acid response element DR1
- The solution structure of the DNA-binding domain of Skn-1
- Rapid isolation of specific DNA-binding proteins and their DNA-binding domains.