Article
Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling.
Molecular and cellular biology - 1 Dec 2007
Riggs Daniel L, Cox Marc B, Tardif Heather L, Hessling Martin, Buchner Johannes, Smith David F
Abstract excerpt
Hormone-dependent transactivation by several of the steroid hormone receptors is potentiated by the Hsp90-associated cochaperone FKBP52, although not by the closely related FKBP51. Here we analyze the mechanisms of potentiation and the functional differences between FKBP51 and FKBP52. While both have peptidyl-prolyl isomerase activity, this is not required for potentiation, as mutations abolishing isomerase...
Topics
- Amino Acid Sequence
- Animals
- Catalysis
- Drug Synergism
- Mice
- Models, Molecular
- Molecular Sequence Data
- Mutant Proteins
- Mutation
- Peptidylprolyl Isomerase
- Protein Structure, Tertiary
- Recombinant Fusion Proteins
- Selection, Genetic