PMID- 26937780
OWN - NLM
STAT- MEDLINE
DCOM- 20160818
LR  - 20190112
IS  - 1520-4995 (Electronic)
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 55
IP  - 12
DP  - 2016 Mar 29
TI  - Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X 
      Receptor alpha in the Context of the Full-Length Protein.
PG  - 1741-1748
LID - 10.1021/acs.biochem.5b01122 [doi]
AB  - 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 RXRalpha 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 
      RXRalpha on DNA and show that the NTD remains highly flexible within this complex.
FAU - Belorusova, Anna
AU  - Belorusova A
AD  - Department of Integrative Structural Biology, Institut de Genetique et de 
      Biologie Moleculaire et Cellulaire (IGBMC), Institut National de la Sante et de 
      la Recherche Medicale (INSERM) U964 / Centre National de la Recherche 
      Scientifique (CNRS) UMR 7104 / Universite de Strasbourg, 67404 Illkirch, France.
FAU - Osz, Judit
AU  - Osz J
AD  - Department of Integrative Structural Biology, Institut de Genetique et de 
      Biologie Moleculaire et Cellulaire (IGBMC), Institut National de la Sante et de 
      la Recherche Medicale (INSERM) U964 / Centre National de la Recherche 
      Scientifique (CNRS) UMR 7104 / Universite de Strasbourg, 67404 Illkirch, France.
FAU - Petoukhov, Maxim V
AU  - Petoukhov MV
AD  - European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, 22603 
      Hamburg, Germany.
FAU - Peluso-Iltis, Carole
AU  - Peluso-Iltis C
AD  - Department of Integrative Structural Biology, Institut de Genetique et de 
      Biologie Moleculaire et Cellulaire (IGBMC), Institut National de la Sante et de 
      la Recherche Medicale (INSERM) U964 / Centre National de la Recherche 
      Scientifique (CNRS) UMR 7104 / Universite de Strasbourg, 67404 Illkirch, France.
FAU - Kieffer, Bruno
AU  - Kieffer B
AD  - Department of Integrative Structural Biology, Institut de Genetique et de 
      Biologie Moleculaire et Cellulaire (IGBMC), Institut National de la Sante et de 
      la Recherche Medicale (INSERM) U964 / Centre National de la Recherche 
      Scientifique (CNRS) UMR 7104 / Universite de Strasbourg, 67404 Illkirch, France.
FAU - Svergun, Dmitri I
AU  - Svergun DI
AD  - European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, 22603 
      Hamburg, Germany.
FAU - Rochel, Natacha
AU  - Rochel N
AD  - Department of Integrative Structural Biology, Institut de Genetique et de 
      Biologie Moleculaire et Cellulaire (IGBMC), Institut National de la Sante et de 
      la Recherche Medicale (INSERM) U964 / Centre National de la Recherche 
      Scientifique (CNRS) UMR 7104 / Universite de Strasbourg, 67404 Illkirch, France.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20160315
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Retinoid X Receptor alpha)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Animals
MH  - Binding Sites/physiology
MH  - Cell Line
MH  - DNA/chemistry/metabolism
MH  - Insecta
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary/physiology
MH  - Retinoid X Receptor alpha/*chemistry/*metabolism
MH  - X-Ray Diffraction
PMC - PMC4968620
MID - EMS69378
OID - NLM: EMS69378
COIS- Notes The authors declare no competing financial interest.
EDAT- 2016/03/05 06:00
MHDA- 2016/08/19 06:00
PMCR- 2016/08/01
CRDT- 2016/03/04 06:00
PHST- 2016/03/04 06:00 [entrez]
PHST- 2016/03/05 06:00 [pubmed]
PHST- 2016/08/19 06:00 [medline]
PHST- 2016/08/01 00:00 [pmc-release]
AID - 10.1021/acs.biochem.5b01122 [doi]
PST - ppublish
SO  - Biochemistry. 2016 Mar 29;55(12):1741-1748. doi: 10.1021/acs.biochem.5b01122. 
      Epub 2016 Mar 15.