Reactome | NCOA3 binds ESR1:estrogen:TFGA gene

NCOA3 binds ESR1:estrogen:TFGA gene

Stable Identifier

R-HSA-9008258

Type

Reaction [binding]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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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 Brzozowski, AM, Pike, AC, Dauter, Z, Hubbard, RE, Bonn, T, Engström, O, Ohman, L, Greene, GL, Gustafsson, JA, Carlquist, M	Nature	1997
25728767	Structure of a biologically active estrogen receptor-coactivator complex on DNA Yi, P, Wang, Z, Feng, Q, Pintilie, GD, Foulds, CE, Lanz, RB, Ludtke, SJ, Schmid, MF, Chiu, W, O'Malley, BW	Mol. Cell	2015