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Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein.

Abstract：

:Retinoid X receptors (RXRs) are transcription factors with important functions in embryonic development, metabolic processes, differentiation, and apoptosis. A particular feature of RXRs is their ability to act as obligatory heterodimerization partners of class II nuclear receptors. At the same time, these receptors are also able to form homodimers that bind to direct repeat separated by one nucleotide hormone response elements. Since the discovery of RXRs, most of the studies focused on its ligand binding and DNA binding domains, while its N-terminal domain (NTD) harboring a ligand-independent activation function remained poorly characterized. Here, we investigated the solution properties of the NTD of RXRα alone and in the context of the full-length receptor using small-angle X-ray scattering and nuclear magnetic resonance spectroscopy. We report the solution structure of the full-length homodimeric RXRα on DNA and show that the NTD remains highly flexible within this complex.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Belorusova A,Osz J,Petoukhov MV,Peluso-Iltis C,Kieffer B,Svergun DI,Rochel N

doi

10.1021/acs.biochem.5b01122

subject

Has Abstract

pub_date

2016-03-29 00:00:00

pages

1741-1748

issue

12

eissn

0006-2960

issn

1520-4995

journal_volume

55

pub_type

杂志文章

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