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TitleStructural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes.
Journal, issue, pagesMol Cell, Vol. 79, Issue 5, Page 812-823.e4, Year 2020
Publish dateSep 3, 2020
AuthorsXinzhe Yu / Ping Yi / Ross A Hamilton / Hong Shen / Muyuan Chen / Charles E Foulds / Michael A Mancini / Steven J Ludtke / Zhao Wang / Bert W O'Malley /
PubMed AbstractSteroid receptors activate gene transcription by recruiting coactivators to initiate transcription of their target genes. For most nuclear receptors, the ligand-dependent activation function domain-2 ...Steroid receptors activate gene transcription by recruiting coactivators to initiate transcription of their target genes. For most nuclear receptors, the ligand-dependent activation function domain-2 (AF-2) is a primary contributor to the nuclear receptor (NR) transcriptional activity. In contrast to other steroid receptors, such as ERα, the activation function of androgen receptor (AR) is largely dependent on its ligand-independent AF-1 located in its N-terminal domain (NTD). It remains unclear why AR utilizes a different AF domain from other receptors despite that NRs share similar domain organizations. Here, we present cryoelectron microscopy (cryo-EM) structures of DNA-bound full-length AR and its complex structure with key coactivators, SRC-3 and p300. AR dimerization follows a unique head-to-head and tail-to-tail manner. Unlike ERα, AR directly contacts a single SRC-3 and p300. The AR NTD is the primary site for coactivator recruitment. The structures provide a basis for understanding assembly of the AR:coactivator complex and its domain contributions for coactivator assembly and transcriptional regulation.
External linksMol Cell / PubMed:32668201 / PubMed Central
MethodsEM (single particle)
Resolution13.0 - 20.0 Å
Structure data

EMDB-22079:
EM Structure of Full-Length Androgen Receptor and DNA Complex
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-22080:
EM Structure of Full-Length Androgen Receptor Coactivator Complex
Method: EM (single particle) / Resolution: 20.0 Å

Source
  • Homo sapiens (human)

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