Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 296, Issue 2, Pages 509-520Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1006/jmbi.1999.3457
Keywords
RXR; transcription factor; DNA-binding; nuclear receptor; structure
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Funding
- NIGMS NIH HHS [GM55217] Funding Source: Medline
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The 9-cis retinoic acid receptor, RXR,binds DNA effectively as a homodimer or as a heterodimer with other nuclear receptors. The DNA-binding sites for these RXR complexes are direct repeats of a consensus sequence. separated by one to five base-pairs of intervening space. Here, we report the 2.1 Angstrom crystal structure df the RXR-DNA-binding domain as a homodimer in complex with its idealized direct repeat DNA target. The structure shows how a gene-regulatory site can induce conformational changes in a transcription factor that promote home-cooperative assembly. Specifically, an alpha-helix in the T-box is disrupted to allow efficient DNA-binding and subunit dimerization. RXR displays a relaxed mode of sequence recognition, interacting with only three base-pairs in each hexameric half-site. The structure illustrates how site selection is achieved in this large eukaryotic transcription factor family through discrete protein-protein interactions and the use of tandem DNA binding;sites with characteristic spacings. (C) 2000 Academic Press.
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