Core LXXLL Motif Sequences in CREB-binding Protein, SRC1, and RIP140 Define Affinity and Selectivity for Steroid and Retinoid Receptors
Open Access
- 1 March 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (9) , 6695-6702
- https://doi.org/10.1074/jbc.m009404200
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Specific Structural Motifs Determine TRAP220 Interactions with Nuclear Hormone ReceptorsMolecular and Cellular Biology, 2000
- The DRIP Complex and SRC-1/p160 Coactivators Share Similar Nuclear Receptor Binding Determinants but Constitute Functionally Distinct ComplexesMolecular and Cellular Biology, 2000
- Structure and specificity of nuclear receptor–coactivator interactionsGenes & Development, 1998
- The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashionProceedings of the National Academy of Sciences, 1998
- The nuclear receptor ligand-binding domain: structure and functionCurrent Opinion in Cell Biology, 1998
- The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathwaysThe EMBO Journal, 1998
- Nuclear Receptor Coactivator ACTR Is a Novel Histone Acetyltransferase and Forms a Multimeric Activation Complex with P/CAF and CBP/p300Cell, 1997
- The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor functionNature, 1997
- A signature motif in transcriptional co-activators mediates binding to nuclear receptorsNature, 1997
- A canonical structure for the ligand-binding domain of nuclear receptorsNature Structural & Molecular Biology, 1996