Structure of the intact PPAR-γ–RXR-α nuclear receptor complex on DNA
Open accessAbstract
Nuclear receptors are multi-domain transcription factors that bind to DNA elements from which they regulate gene expression. The peroxisome proliferator-activated receptors (PPARs) form heterodimers with the retinoid X receptor (RXR), and PPAR-gamma has been intensively studied as a drug target because of its link to insulin sensitization. Previous structural studies have focused on isolated DNA or ligand-binding segments, with no demonstration of how multiple domains cooperate to modulate receptor properties. Here we present structures of intact PPAR-gamma and RXR-alpha as a heterodimer bound to DNA, ligands and coactivator peptides. PPAR-gamma and RXR-alpha form a non-symmetric complex, allowing the ligand-binding domain (LBD) of PPAR-gamma to contact multiple domains in both proteins. Three interfaces link PPAR-gamma and RXR-alpha, including some that are DNA dependent. The PPAR-gamma LBD cooperates with both DNA-binding domains (DBDs) to enhance response-element binding. The A/B segments are highly dynamic, lacking folded substructures despite their gene-activation properties.
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Previously published full-length nuclear hormone receptor structures do not present NTD information.
“Previously published full-length nuclear hormone receptor structures (Chandra et al., 2008; Chandra et al., 2013; Lou et al., 2014; Orlov et al., 2012) also do not present any NTD information.”
From Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes (2020) · cites this paper as Chandra et al., 2008
The LBD-DBD domain arrangement is similar to the HNF4α dimer and different from the non-symmetric PPARγ-RXRα dimer or the X-shape LBD-DBD crossing arrangement in the RXRα-LXRβ dimer.
“This LBD-DBD domain arrangement is similar to the HNF4α dimer that was solved by X-ray crystallography (Chandra et al., 2013), which is different from the non-symmetric PPARγ-RXRα dimer (Chandra et al., 2008) or the X-shape LBD-DBD crossing arrangement in RXRα-LXRβ dimer (Lou et al., 2014).”
From Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes (2020) · cites this paper as Chandra et al., 2008
AnSRs exist as obligate dimers, exhibit less flexibility, and maintain binding to repeat consensus sequences in vivo (70%).
“AnSRs that exist as obligate dimers, exhibit less flexibility, and maintain binding to repeat consensus sequences in vivo (70%)”
From Allosteric interactions prime androgen receptor dimerization and activation (2022) · cites this paper as Chandra et al., 2008
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“This scenario is in contrast to that of the AnSRs that exist as obligate dimers, exhibit less flexibility, and maintain binding to repeat consensus sequences in vivo (70%), even in the presence of oncoprotein cofactors (Arruabarrena-Aristorena et al., 2020; Chandra et al., 2008; Chandra et al., 2013; Chandra et al., 2…”
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- Authors
- Chandra, V., Huang, P., Hamuro, Y., Raghuram, S., Wang, Y., Burris, T. P., & Rastinejad, F.
- Affiliations
- University of Virginia Health System (US)
- Pennington Biomedical Research Center (US)
- Venue
- Nature
- Published
- 2008-11
- Volume
- 456
- Issue
- 7220
- Pages
- 350-356
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2743566
- OpenAlex
- W2105259330
- Cited by
- 808
- References
- 52
- Citations by year
- 2026: 25 · 2025: 41 · 2024: 46 · 2023: 42 · 2022: 51 · 2021: 39 · 2020: 42 · 2019: 36 · 2018: 45 · 2017: 41 · 2016: 36 · 2015: 59 · 2014: 55 · 2013: 48 · 2012: 49
- FWCI
- 21.09
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Lirias (KU Leuven) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM055217)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- PPARγ, RXRα, nuclear receptor heterodimers, DNA binding, ligand-binding domain, DNA-binding domain, coactivator peptide, insulin sensitization, transcription factor structure
- MeSH terms
- Allosteric Regulation, Base Sequence, DNA, Humans, Ligands, Models, Molecular, Protein Binding, Protein Structure, Tertiary, Response Elements, Multiprotein Complexes, Retinoid X Receptor alpha, PPAR gamma, Protein Multimerization
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