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TitleInterplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression.
Journal, issue, pagesStructure, Vol. 27, Issue 8, Page 1270-11285.e6, Year 2019
Publish dateAug 6, 2019
AuthorsTiago N Cordeiro / Nathalie Sibille / Pierre Germain / Philippe Barthe / Abdelhay Boulahtouf / Fréderic Allemand / Rémy Bailly / Valérie Vivat / Christine Ebel / Alessandro Barducci / William Bourguet / Albane le Maire / Pau Bernadó /
PubMed AbstractIn its unliganded form, the retinoic acid receptor (RAR) in heterodimer with the retinoid X receptor (RXR) exerts a strong repressive activity facilitated by the recruitment of transcriptional ...In its unliganded form, the retinoic acid receptor (RAR) in heterodimer with the retinoid X receptor (RXR) exerts a strong repressive activity facilitated by the recruitment of transcriptional corepressors in the promoter region of target genes. By integrating complementary structural, biophysical, and computational information, we demonstrate that intrinsic disorder is a required feature for the precise regulation of RAR activity. We show that structural dynamics of RAR and RXR H12 regions is an essential mechanism for RAR regulation. Unexpectedly we found that, while mainly disordered, the corepressor N-CoR presents evolutionary conserved structured regions involved in transient intramolecular contacts. In the presence of RXR/RAR, N-CoR exploits its multivalency to form a cooperative multisite complex that displays equilibrium between different conformational states that can be tuned by cognate ligands and receptor mutations. This equilibrium is key to preserving the repressive basal state while allowing the conversion to a transcriptionally active form.
External linksStructure / PubMed:31178221
MethodsSAS (X-ray synchrotron)
Structure data

SASDF34: Free Nuclear receptor CoRepressor NID (spanning from residue Gln2059 to Glu2325)
Method: SAXS/SANS

SASDF44: RXR/RAR Heterodimer : N-CoRNID Complex (1:1) (Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID), N-CoR-NID + Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD), RXR + Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB), RAR)
Method: SAXS/SANS

SASDF54: RXRΔH12/RAR Heterodimer : N-CoRNID Complex (1:1)
Method: SAXS/SANS

SASDF64: RXR/RAR Heterodimer : N-CoRNID Complex (1:1) with RAR inverse agonist (BMS493)
Method: SAXS/SANS

SASDF74: RXR/RARI396E Heterodimer : N-CoRNID Complex (1:1)
Method: SAXS/SANS

SASDF84: RXR/RAR Heterodimer : N-CoRNID Complex (1:1) with RAR agonist (Am580)
Method: SAXS/SANS

Source
  • Mouse (mice)
  • Human (human)

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