+Search query
-Structure paper
Title | Structure of a biologically active estrogen receptor-coactivator complex on DNA. |
---|---|
Journal, issue, pages | Mol Cell, Vol. 57, Issue 6, Page 1047-1058, Year 2015 |
Publish date | Mar 19, 2015 |
Authors | Ping Yi / Zhao Wang / Qin Feng / Grigore D Pintilie / Charles E Foulds / Rainer B Lanz / Steven J Ludtke / Michael F Schmid / Wah Chiu / Bert W O'Malley / |
PubMed Abstract | Estrogen receptor (ER/ESR1) is a transcription factor critical for development, reproduction, metabolism, and cancer. ER function hinges on its ability to recruit primary and secondary coactivators, ...Estrogen receptor (ER/ESR1) is a transcription factor critical for development, reproduction, metabolism, and cancer. ER function hinges on its ability to recruit primary and secondary coactivators, yet structural information on the full-length receptor-coactivator complex to complement preexisting and sometimes controversial biochemical information is lacking. Here, we use cryoelectron microscopy (cryo-EM) to determine the quaternary structure of an active complex of DNA-bound ERα, steroid receptor coactivator 3 (SRC-3/NCOA3), and a secondary coactivator (p300/EP300). Our structural model suggests the following assembly mechanism for the complex: each of the two ligand-bound ERα monomers independently recruits one SRC-3 protein via the transactivation domain of ERα; the two SRC-3s in turn bind to different regions of one p300 protein through multiple contacts. We also present structural evidence for the location of activation function 1 (AF-1) in a full-length nuclear receptor, which supports a role for AF-1 in SRC-3 recruitment. |
External links | Mol Cell / PubMed:25728767 / PubMed Central |
Methods | EM (single particle) |
Resolution | 25.0 - 47.0 Å |
Structure data | EMDB-6241: EMDB-6259: EMDB-6260: EMDB-6261: EMDB-6262: EMDB-6263: EMDB-6264: |
Source |
|