The orphan nuclear receptor SHP utilizes conserved LXXLL-related motifs for interactions with ligand-activated estrogen receptors

Molecular and Cellular Biology

Volumn 20, Issue 4, 2000, Pages 1124-1133

  Johansson, Lotta ^a   Båvner, Ann ^a   Thomsen, Jane S ^a   Färnegårdh, Mathias ^b   Gustafsson, Jan Åke ^a   Treuter, Eckardt ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b Karo Bio   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; DNA; ESTROGEN RECEPTOR; GLUTATHIONE TRANSFERASE;

ARTICLE; CONTROLLED STUDY; DIMERIZATION; DNA BINDING; HUMAN; HUMAN CELL; LIGAND BINDING; MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; RECEPTOR BINDING; SIGNAL TRANSDUCTION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; CONSERVED SEQUENCE; DIMERIZATION; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; HUMANS; LIGANDS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, QUATERNARY; RATS; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, ESTROGEN; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0342980409     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.4.1124-1133.2000     Document Type: Article

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