Estrogen activity domains

Norris, J.D., Fan, D., Kerner, S.A. and McDonnell, D.P. (1997) Identification of a third autonomous activation domain within the human estrogen receptor. Molecular Endocrinology, 11, 747-754. 

Watanabe, M. Yanagisawa, )., Kitagawa, H., et al. 2001. A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor a coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA. EMBO J. 20, 1341-1352. 

The AF-1 domain in ERa is very active on a variety of estrogen responsive promoters, whereas the AF-1 is only minimally active in ER/3 [19]. 

Due to the complex structure of the initiation complex it remains imclear which interactions are responsible for the first mechanism. The coupling between the transactivat-ing domain and the initiation complex can be direct or indirect. There is evidence which indicates that proteins with co-activator function mediate the interaction between HRE-bound receptors and the transcription initiation apparatus. One such protein is RIP-140, which mediates the transcription activation of the estrogen receptor. The AF2 domain can also directly contact the transcriptional apparatus. One component of the RNA polymerase II holoenzyme, the SUGl protein, has been identified as a binding partner for the AF2 domain. The SUGl protein has the function of a co-acti-vator in transcription initiation and is considered a mediator (see 1.4.3.2). 

Lewis, D.F.V. et al. (2002) Molecular modelling of the human glucocorticoid receptor (hGR) ligand-binding domain (LBD) by homology with the human estrogen receptor a (hERa) LBD quantitative structure-activity... 

Montano, M. M., Muller, V., Trobaugh, A., and Katzenellenboger, B. S. 1995. The carboxy-terminal F domain of the human estrogen receptor Role in the transcriptional activity of the receptor and the effectiveness of antiestrogens as estrogen antigonists. Mol. Endocrinol. 9 814—825. 

Feil, R., Wagner, J., Metzger, D., and Chambon, P. (1997) Regulation of Cre recombinase activity by mutated estrogen receptor ligand-binding domains. Biochem. Biophys. Res. Commun. 237, 752-757. 

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