The human estrogen receptor α dimer binds a single SRC-1 coactivator molecule with an affinity dictated by agonist structure

Journal of Molecular Biology

Volumn 306, Issue 3, 2001, Pages 433-442

  Margeat, Emmanuel ^a   Poujol, Nicolas ^a   Boulahtouf, Abdelhay ^b   Chen, Yan ^c   Müller, Joachim D ^c   Gratton, Enrico ^c   Cavailles, Vincent ^b   Royer, Catherine A ^a  

^a CNRS   (France)

^b INSERM   (France)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Affinity; Coactivator; Estrogen receptor; Fluorescence; Photon counting histogram

Indexed keywords

CELL NUCLEUS RECEPTOR; DIMER; ESTROGEN RECEPTOR ALPHA; ESTRONE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SRC 1; UNCLASSIFIED DRUG;

ANISOTROPY; ARTICLE; BINDING AFFINITY; CHEMICAL STRUCTURE; COMPLEX FORMATION; FLUORESCENCE SPECTROSCOPY; GENETIC TRANSCRIPTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; STOICHIOMETRY;

UNIDENTIFIED BACULOVIRUS;

EID: 0035936687     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4418     Document Type: Article

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