The autonomous transactivation domain in helix H3 of the vitamin D receptor is required for transactivation and coactivator interaction

Journal of Biological Chemistry

Volumn 274, Issue 20, 1999, Pages 14352-14358

  Kraichely, Dennis M ^a   Collins III, John J ^a   DeLisle, Robert K ^a   MacDonald, Paul N ^a,b  

^a SAINT LOUIS UNIVERSITY   (United States)

^b SAINT LOUIS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCITRIOL; VITAMIN D RECEPTOR;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CRYSTALLOGRAPHY; IMMUNOASSAY; LIGAND BINDING; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; TRANSACTIVATION; TRANSCRIPTION REGULATION; VITAMIN METABOLISM; YEAST;

ANIMALS; BINDING SITES; CALCITRIOL; COS CELLS; CRYSTALLOGRAPHY, X-RAY; FURYLFURAMIDE; HELIX-LOOP-HELIX MOTIFS; LIGANDS; MUTAGENESIS, SITE-DIRECTED; NUCLEAR RECEPTOR COACTIVATOR 2; POINT MUTATION; RECEPTORS, CALCITRIOL; RECEPTORS, RETINOIC ACID; RETINOID X RECEPTORS; STRUCTURE-ACTIVITY RELATIONSHIP; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS;

ANIMALIA; MAMMALIA;

EID: 0033553422     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.20.14352     Document Type: Article

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