Small-Angle X-ray Scattering Studies on Structures of an Estrogen-Related Receptor α Ligand Binding Domain and Its Complexes with Ligands and Coactivators

2008 ◽  
Vol 112 (32) ◽  
pp. 9603-9612 ◽  
Author(s):  
Kyeong Sik Jin ◽  
Joon Kyu Park ◽  
Jinhwan Yoon ◽  
Yecheol Rho ◽  
Jae-Hong Kim ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Small Angle ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
X Ray ◽  
X Ray Scattering ◽  
Estrogen Related Receptor ◽  
Ray Scattering

scholarly journals Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D

2021 ◽  
Vol 41 (1) ◽  
Author(s):  
Claudia S. Kielkopf ◽  
Andrew E. Whitten ◽  
Brett Garner ◽  
Simon H.J. Brown
Keyword(s):  
Ligand Binding ◽  
Conformational Changes ◽  
Small Angle ◽  
Protective Role ◽  
Oligomeric State ◽  
Experimental Conditions ◽  
X Ray ◽  
X Ray Scattering ◽  
Apolipoprotein D ◽  
Ray Scattering

Abstract Human apolipoprotein-D (apoD) is a glycosylated lipocalin that plays a protective role in Alzheimer’s disease due to its antioxidant function. Native apoD from human body fluids forms oligomers, predominantly a stable tetramer. As a lipocalin, apoD binds and transports small hydrophobic molecules such as progesterone, palmitic acid and sphingomyelin. Oligomerisation is a common trait in the lipocalin family and is affected by ligand binding in other lipocalins. The crystal structure of monomeric apoD shows no major changes upon progesterone binding. Here, we used small-angle X-ray scattering (SAXS) to investigate the influence of ligand binding and oxidation on apoD oligomerisation and conformation. As a solution-based technique, SAXS is well suited to detect changes in oligomeric state and conformation in response to ligand binding. Our results show no change in oligomeric state of apoD and no major conformational changes or subunit rearrangements in response to binding of ligands or protein oxidation. This highlights the highly stable structure of the native apoD tetramer under various physiologically relevant experimental conditions.

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