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The quaternary architecture of RARβ-RXRα heterodimer facilitates domain-domain signal transmission

Chandra, Vikas ; Wu, Dalei ; Li, Sheng ; Potluri, Nalini ; Kim, Youngchang ; Rastinejad, Fraydoon

Nature Communications, 2017-10, Vol.8 (1) [Periódico revisado por pares]

NATURE PUBLISHING GROUP

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  • Título:
    The quaternary architecture of RARβ-RXRα heterodimer facilitates domain-domain signal transmission
  • Autor: Chandra, Vikas ; Wu, Dalei ; Li, Sheng ; Potluri, Nalini ; Kim, Youngchang ; Rastinejad, Fraydoon
  • É parte de: Nature Communications, 2017-10, Vol.8 (1)
  • Descrição: Assessing the physical connections and allosteric communications in multi-domain nuclear receptor (NR) polypeptides has remained challenging, with few crystal structures available to show their overall structural organizations. Here we report the quaternary architecture of multi-domain retinoic acid receptor β-retinoic X receptor α (RARβ-RXRα) heterodimer bound to DNA, ligands and coactivator peptides, examined through crystallographic, hydrogen-deuterium exchange mass spectrometry, mutagenesis and functional studies. The RARβ ligand-binding domain (LBD) and DNA-binding domain (DBD) are physically connected to foster allosteric signal transmission between them. Direct comparisons among all the multi-domain NRs studied crystallographically to date show significant variations within their quaternary architectures, rather than a common architecture adhering to strict rules. RXR remains flexible and adaptive by maintaining loosely organized domains, while its heterodimerization partners use a surface patch on their LBDs to form domain-domain interactions with DBDs.Nuclear receptors (NR) are multidomain proteins, which makes their crystallization challenging. Here the authors present the crystal structure of the retinoic acid receptor β-retinoic X receptor α (RARβ-RXRα) heterodimer bound to DNA, ligands and coactivator peptides, which shows that NR quaternary architectures are variable.
  • Editor: NATURE PUBLISHING GROUP
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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