Summary information and primary citation
- PDB-id
-
1dsz;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcription-DNA
- Method
- X-ray (1.7 Å)
- Summary
- Structure of the rxr-rar DNA-binding domain heterodimer
in complex with the retinoic acid response element dr1
- Reference
-
Rastinejad F, Wagner T, Zhao Q, Khorasanizadeh S (2000):
"Structure
of the RXR-RAR DNA-binding complex on the retinoic acid
response element DR1." EMBO J.,
19, 1045-1054. doi: 10.1093/emboj/19.5.1045.
- Abstract
- The 9-cis retinoic acid receptor (retinoid X receptor,
RXR) forms heterodimers with the all-trans retinoic acid
receptor (RAR) and other nuclear receptors on DNA
regulatory sites composed of tandem binding elements. We
describe the 1.70 A resolution structure of the ternary
complex of RXR and RAR DNA-binding regions in complex with
the retinoic acid response element DR1. The receptors
recognize identical half-sites through extensive
base-specific contacts; however, RXR binds exclusively to
the 3' site to form an asymmetric complex with the reverse
polarity of other RXR heterodimers. The subunits associate
in a strictly DNA-dependent manner using the T-box of RXR
and the Zn-II region of RAR, both of which are reshaped in
forming the complex. The protein-DNA contacts, the
dimerization interface and the DNA curvature in the RXR-RAR
complex are distinct from those of the RXR homodimer, which
also binds DR1. Together, these structures illustrate how
the nuclear receptor superfamily exploits conformational
flexibility and locally induced structures to generate
combinatorial transcription factors.