NCOA3 recruits EP300 to ESR1:estrogen:TFGA gene:NCOA3

Stable Identifier
R-HSA-9008285
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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). A structural model 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
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
Participants
Participates
Orthologous Events
Authored
Reviewed
Created
Cite Us!