PMID- 25645674
OWN - NLM
STAT- MEDLINE
DCOM- 20151201
LR  - 20230106
IS  - 2045-2322 (Electronic)
IS  - 2045-2322 (Linking)
VI  - 5
DP  - 2015 Feb 3
TI  - Structural basis of natural promoter recognition by the retinoid X nuclear 
      receptor.
PG  - 8216
LID - 10.1038/srep08216 [doi]
LID - 8216
AB  - Retinoid X receptors (RXRs) act as homodimers or heterodimerisation partners of 
      class II nuclear receptors. RXR homo- and heterodimers bind direct repeats of the 
      half-site (A/G)G(G/T)TCA separated by 1 nucleotide (DR1). We present a structural 
      characterization of RXR-DNA binding domain (DBD) homodimers on several natural 
      DR1s and an idealized symmetric DR1. Homodimers displayed asymmetric binding, 
      with critical high-affinity interactions accounting for the 3' positioning of RXR 
      in heterodimers on DR1s. Differing half-site and spacer DNA sequence induce 
      changes in RXR-DBD homodimer conformation notably in the dimerization interface 
      such that natural DR1s are bound with higher affinity than an idealized symmetric 
      DR1. Subtle changes in the consensus DR1 DNA sequence therefore specify binding 
      affinity through altered RXR-DBD-DNA contacts and changes in DBD conformation 
      suggesting a general model whereby preferential half-site recognition determines 
      polarity of heterodimer binding to response elements.
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 - McEwen, Alastair G
AU  - McEwen AG
AD  - Structural Biology Platform, 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 - Poussin-Courmontagne, Pierre
AU  - Poussin-Courmontagne P
AD  - Structural Biology Platform, 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 - Moutier, Emmanuel
AU  - Moutier E
AD  - Department of Functional Genomics and Cancer, 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 - Birck, Catherine
AU  - Birck C
AD  - Structural Biology Platform, 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 - Davidson, Irwin
AU  - Davidson I
AD  - Department of Functional Genomics and Cancer, 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 - Moras, Dino
AU  - Moras D
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 - 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
SI  - PDB/4CN2
SI  - PDB/4CN3
SI  - PDB/4CN5
SI  - PDB/4CN7
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20150203
PL  - England
TA  - Sci Rep
JT  - Scientific reports
JID - 101563288
RN  - 0 (Retinoid X Receptors)
SB  - IM
MH  - Base Sequence
MH  - Binding Sites
MH  - Calorimetry
MH  - Crystallography, X-Ray
MH  - Dimerization
MH  - Humans
MH  - Molecular Dynamics Simulation
MH  - Nucleic Acid Conformation
MH  - Promoter Regions, Genetic
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Response Elements/genetics
MH  - Retinoid X Receptors/chemistry/*genetics/metabolism
PMC - PMC4314640
EDAT- 2015/02/04 06:00
MHDA- 2015/12/15 06:00
PMCR- 2015/02/03
CRDT- 2015/02/04 06:00
PHST- 2014/10/20 00:00 [received]
PHST- 2014/12/29 00:00 [accepted]
PHST- 2015/02/04 06:00 [entrez]
PHST- 2015/02/04 06:00 [pubmed]
PHST- 2015/12/15 06:00 [medline]
PHST- 2015/02/03 00:00 [pmc-release]
AID - srep08216 [pii]
AID - 10.1038/srep08216 [doi]
PST - epublish
SO  - Sci Rep. 2015 Feb 3;5:8216. doi: 10.1038/srep08216.