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Details on Person X-ray crystallography studies illustrated that the ligand-bo...

Class:IdSummation:9008248
_displayNameX-ray crystallography studies illustrated that the ligand-bo...
_timestamp2017-10-02 19:31:23
created[InstanceEdit:9008276] Shamovsky, Veronica, 2017-06-08
literatureReference[LiteratureReference:9008241] Structure of a biologically active estrogen receptor-coactivator complex on DNA
[LiteratureReference:9008243] Molecular basis of agonism and antagonism in the oestrogen receptor
modified[InstanceEdit:9024236] Rothfels, Karen, 2017-10-02
textX-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).
(summation)[Reaction:9008258] NCOA3 binds ESR1:estrogen:TFGA gene [Homo sapiens]
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