A ternary switch model governing ERĪ± ligand binding domain conformation.

McDougal DP, Pederick JL, Novick SJ, Jovcevski B, Warrender AK, Pascal BD, Griffin PR, Bruning JB, Nat Commun 16(1):10363 (2025) Europe PMC

SASDWC7 – SEC-SAXS data of wildtype human apo estrogen receptor alpha ligand binding domain (LBD) at pH 7.5

Estrogen receptor alpha
MWexperimental 58 kDa
MWexpected 55 kDa
VPorod 74 nm3
log I(s) 7.33×10-3 7.33×10-4 7.33×10-5 7.33×10-6
Estrogen receptor alpha small angle scattering data  s, nm-1
ln I(s)
Estrogen receptor alpha Guinier plot ln 7.33×10-3 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Estrogen receptor alpha Kratky plot 1.104 0 √3 sRg
p(r)
Estrogen receptor alpha pair distance distribution function Rg: 2.4 nm 0 Dmax: 7.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Estrogen receptor alpha DAMMIF model
Synchrotron SAXS data from solutions of SEC-SAXS data of wildtype human apo estrogen receptor alpha ligand binding domain (LBD) at pH 7.5 in 20 mM Tris-HCl pH 7.5, 150 mM NaCl, 5% glycerol, 2 mM TCEP, pH 7.5 were collected on the BioSAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus3 X 2M detector at a sample-detector distance of 2.2 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 80.00 μl sample at 5 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 19.8°C. 641 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Estrogen receptor alpha
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   27.6 kDa
 
UniProt   P03372 (310-549)
Sequence   FASTA