Article
A tetratricopeptide repeat half-site in the aryl hydrocarbon receptor is important for DNA binding and trans-activation potential.
Molecular pharmacology - 1 Dec 2000
Levine S L, Petrulis J R, Dubil A, Perdew G H
Abstract excerpt
Similar to certain unliganded steroid hormone receptor complexes, the unliganded aryl hydrocarbon receptor has been shown to consist of a multimeric core complex that includes the 90-kDa heat shock protein (hsp90) and the immunophilin-like hepatitis B X-associated protein 2 (XAP2). Immunophilins and XAP2 associated with these complexes bind to the carboxyl-terminal end of hsp90 through an interaction with their...
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- COS Cells
- Cell Line
- DNA
- DNA, Complementary
- Dimerization
- HSP90 Heat-Shock Proteins
- Intracellular Signaling Peptides and Proteins
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Protein Binding
