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The nuclear hormone receptors form the largest known family of transcription factors. The current notion of receptor DNA discrimination, based solely on one major type of hexameric half-site and a highly conserved 66-residue core DNA-binding domain (DBD), does not adequately describe how more than 150 nonsteroid receptors differentiate among response elements. Here, we describe the 2.3 A crystal structure of the DNA-binding region of the orphan receptor RevErb arranged as a tandem homodimer on its optimal response element. The structure reveals the presence of a second major protein-DNA interface adjacent to the classical one involving the half-sites. A sequence comparison of orphan receptors suggests that unique minor-groove interactions involving the receptor hinge regions impart the necessary DNA and dimerization specificity.

Original publication

DOI

10.1016/s1097-2765(00)80084-2

Type

Journal article

Journal

Molecular cell

Publication Date

05/1998

Volume

1

Pages

849 - 861

Addresses

Department of Pharmacology, School of Medicine, University of Virginia, Charlottesville 22908, USA.

Keywords

Humans, Proteins, DNA-Binding Proteins, Nuclear Proteins, Receptors, Cytoplasmic and Nuclear, Receptors, Steroid, DNA, Crystallography, Binding Sites, Conserved Sequence, Nucleic Acid Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Image Processing, Computer-Assisted, Molecular Sequence Data, Nuclear Receptor Subfamily 1, Group D, Member 1