Summary information and primary citation
- PDB-id
-
1ga5;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcription-DNA
- Method
- X-ray (2.4 Å)
- Summary
- Crystal structure of the orphan nuclear receptor
rev-erb(alpha) DNA-binding domain bound to its cognate
response element
- Reference
-
Sierk ML, Zhao Q, Rastinejad F (2001): "DNA
Deformability as a Recognition Feature in the RevErb
Response Element." Biochemistry,
40, 12833-12843. doi: 10.1021/bi011086r.
- Abstract
- Most nuclear receptors recognize the same consensus
hexameric sequence, AGGTCA. An important question has been
how the various members of this transcription factor family
distinguish identity features in these closely related DNA
sites. We determined structures from several crystal forms
of the RevErb-DNA complex and analyzed the patterns of
protein-DNA interactions and DNA distortions. We found a
significant and consistent DNA distortion at a TA step
directly preceding the first consensus 5'-AGGTCA-3'
recognition sequence. Importantly, while this base-pair
sequence is associated with RevErb's high-affinity sites,
there are no sequence-specific contacts formed with the
protein. Our study shows that RevErb relies instead on the
intrinsic geometry and flexibility of this TA site to make
the required fit between the proteins' independent major
groove and minor groove binding interactions, which occur
on both sides of the TA step. Our findings extend the
description of response element discrimination to include a
role for sequence-dependent DNA deformations and suggest
how other monomeric members of this superfamily, such as
NGFI-B, SF-1, and ROR, could also recognize unique
geometric features in their DNA targets.
