1BY4
STRUCTURE AND MECHANISM OF THE HOMODIMERIC ASSEMBLY OF THE RXR ON DNA
Summary for 1BY4
Entry DOI | 10.2210/pdb1by4/pdb |
Descriptor | DNA (5'-D(*C*TP*AP*GP*GP*TP*CP*AP*AP*AP*GP*GP*TP*CP*AP*G)-3'), DNA (5'-D(*CP*TP*GP*AP*CP*CP*TP*TP*TP*GP*AP*CP*CP*TP*A)-3'), PROTEIN (RETINOIC ACID RECEPTOR RXR-ALPHA), ... (5 entities in total) |
Functional Keywords | rxr, nuclear receptor, hormone response element, protein-dna interations, gene regulation-dna complex, gene regulation/dna |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: P19793 |
Total number of polymer chains | 8 |
Total formula weight | 58062.46 |
Authors | Zhao, Q.,Chasse, S.A.,Devarakonda, S.,Sierk, M.L.,Ahvazi, B.,Sigler, P.B.,Rastinejad, F. (deposition date: 1998-10-22, release date: 2000-01-12, Last modification date: 2023-08-09) |
Primary citation | Zhao, Q.,Chasse, S.A.,Devarakonda, S.,Sierk, M.L.,Ahvazi, B.,Rastinejad, F. Structural basis of RXR-DNA interactions. J.Mol.Biol., 296:509-520, 2000 Cited by PubMed Abstract: 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 A crystal structure of 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 homo-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. PubMed: 10669605DOI: 10.1006/jmbi.1999.3457 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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