NCOA3 binds ESR1:estrogen:TFGA gene

Stable Identifier
Reaction [binding]
Homo sapiens
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X-ray crystallography studies illustrated that the ligand-bound ESR1 interacts with LXXLL motif-containing NCOA3 (SRC3) through the ligand-binding domain (LBD) at the C-terminus of ESR1, which also has a ligand-dependent transactivation function (known as AF-2) (Brzozowski et al. 1997). Cryoelectron microscopy (cryo-EM) determined the quaternary structure of an active complex of DNA-bound ESR1, steroid receptor coactivator 3 (SRC3 or NCOA3), and a secondary coactivator (p300/EP300). Structural models suggests the following assembly mechanism for the complex: each of the two ligand-bound ESR1 monomers independently recruits one NCOA3 protein via the transactivation domain of ESR1;the two NCOA3s in turn bind to different regions of one p300 protein through multiple contacts (Yi P et al. 2015).

Literature References
PubMed ID Title Journal Year
9338790 Molecular basis of agonism and antagonism in the oestrogen receptor

Carlquist, M, Brzozowski, AM, Bonn, T, Dauter, Z, Gustafsson, JA, Greene, GL, Pike, AC, Engström, O, Ohman, L, Hubbard, RE

Nature 1997
25728767 Structure of a biologically active estrogen receptor-coactivator complex on DNA

O'Malley, BW, Pintilie, GD, Foulds, CE, Yi, P, Ludtke, SJ, Lanz, RB, Feng, Q, Chiu, W, Schmid, MF, Wang, Z

Mol. Cell 2015
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