Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains.

Huang W, Peng Y, Kiselar J, Zhao X, Albaqami A, Mendez D, Chen Y, Chakravarthy S, Gupta S, Ralston C, Kao HY, Chance MR, Yang S
Nat Commun 9(1):3520 (2018 Aug 30)

PMID: 30166540 doi: 10.1038/s41467-018-06034-2

Submitted to SASBDB: 2018 Jun 22 Published in SASBDB: 2018 Sep 1

SASDDU8 – Multidomain architecture of the estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains Sample: Estrogen receptor dimer, 85 kDa protein ERE1 monomer, 6 kDa Homo sapiens DNA ERE2 monomer, 6 kDa Homo sapiens DNA Estradiol dimer, 0 kDa HERa peptide1 monomer, 2 kDa protein HERa peptide2 monomer, 2 kDa protein Buffer: 10 mM CHES (pH9.5), 125 mM NaCl, 5mM KCl, 4 mM MgCl2, 50 mM arginine, 50 mM glutamate, 5 mM TCEP, 5% glycerol, 10 µm Zn acetate, 10 µM estradiol, pH: 9.5 Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Aug 10 RgGuinier 3.8 nm Dmax 11.5 nm