Structural basis for DNA recognition and allosteric control of the retinoic acid receptors RAR–RXR

Osz J, McEwen A, Bourguet M, Przybilla F, Peluso-Iltis C, Poussin-Courmontagne P, Mély Y, Cianférani S, Jeffries C, Svergun D, Rochel N
Nucleic Acids Research (2020 Aug 25)

doi: 10.1093/nar/gkaa697

Submitted to SASBDB: 2020 Jun 24 Published in SASBDB: 2020 Aug 11

SASDFT8 – The retinoic acid receptor (RAR-RXR heterodimer) bound to the DNA response element HoxB13 DR0 Sample: Retinoic acid receptor alpha, RAR monomer, 41 kDa Mus musculus protein Retinoic acid receptor RXR-alpha monomer, 38 kDa Mus musculus protein DNA response element HoxB13 DR0 monomer, 10 kDa DNA Buffer: 20 mM Tris, pH 8, 150 mM NaCl, 5% v/v glycerol, 1 mM CHAPS, 4 mM MgSO4, 1 mM TCEP, pH: 8 Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 19 RgGuinier 3.8 nm Dmax 14.5 nm VolumePorod 132 nm3

SASDFU8 – The retinoic acid receptor (RAR-RXR heterodimer) bound to the DNA response element F11r DR5. Sample: Retinoic acid receptor alpha, RAR monomer, 41 kDa Mus musculus protein Retinoic acid receptor RXR-alpha monomer, 38 kDa Mus musculus protein DNA response element F11r DR5 monomer, 13 kDa DNA Buffer: 20 mM Tris, pH 8, 150 mM NaCl, 5% v/v glycerol, 1 mM CHAPS, 4 mM MgSO4, 1 mM TCEP, pH: 8 Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 19 RgGuinier 4.0 nm Dmax 13.5 nm VolumePorod 130 nm3