scholarly journals Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase.

2003 ◽  
Vol 111 (7) ◽  
pp. 884-888 ◽  
Author(s):  
Sergei Shevtsov ◽  
Evgeniy V Petrotchenko ◽  
Lars C Pedersen ◽  
Masahiko Negishi
Keyword(s):  
Binding Site ◽  
Polychlorinated Biphenyl ◽  
Crystallographic Analysis ◽  
Estrogen Sulfotransferase ◽  
Estrogen Binding

scholarly journals A potent and selective photoaffinity probe for the anti-estrogen binding site of rat liver.

1990 ◽  
Vol 265 (28) ◽  
pp. 17039-17043
Author(s):  
M Poirot ◽  
C Chailleux ◽  
A Fargin ◽  
F Bayard ◽  
J C Faye
Keyword(s):  
Binding Site ◽  
Rat Liver ◽  
Estrogen Binding

scholarly journals Mitigating the Adverse Effects of Polychlorinated Biphenyl Derivatives on Estrogenic Activity via Molecular Modification Techniques

2021 ◽  
Vol 18 (9) ◽  
pp. 4999
Author(s):  
Wei He ◽  
Wenhui Zhang ◽  
Zhenhua Chu ◽  
Yu Li
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Hydrophobic Interaction ◽  
Oestrogen Receptor ◽  
Polychlorinated Biphenyl ◽  
Hydrophobic Interactions ◽  
Estrogenic Activity ◽  
Average Distance ◽  
Amino Acid Residues ◽  
Hydrophobic Amino Acid

The aim of this paper is to explore the mechanism of the change in oestrogenic activity of PCBs molecules before and after modification by designing new PCBs derivatives in combination with molecular docking techniques through the constructed model of oestrogenic activity of PCBs molecules. We found that the weakened hydrophobic interaction between the hydrophobic amino acid residues and hydrophobic substituents at the binding site of PCB derivatives and human oestrogen receptor alpha (hERα) was the main reason for the weakened binding force and reduced anti-oestrogenic activity. It was consistent with the information that the hydrophobic field displayed by the 3D contour maps in the constructed oestrogen activity CoMSIA model was one of the main influencing force fields. The hydrophobic interaction between PCB derivatives and oestrogen-active receptors was negatively correlated with the average distance between hydrophobic substituents and hydrophobic amino acid residues at the hERα-binding site, and positively correlated with the number of hydrophobic amino acid residues. In other words, the smaller the average distance between the hydrophobic amino acid residues at the binding sites between the two and the more the number of them, and the stronger the oestrogen activity expression degree of PCBS derivative molecules. Therefore, hydrophobic interactions between PCB derivatives and the oestrogen receptor can be reduced by altering the microenvironmental conditions in humans. This reduces the ability of PCB derivatives to bind to the oestrogen receptor and can effectively modulate the risk of residual PCB derivatives to produce oestrogenic activity in humans.

scholarly journals Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site

Crystals ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 375 ◽  
Author(s):  
Tatyana Prudnikova ◽  
Barbora Kascakova ◽  
Jeroen R. Mesters ◽  
Pavel Grinkevich ◽  
Petra Havlickova ◽  
...  
Keyword(s):  
Binding Site ◽  
Data Bank ◽  
Crystallographic Analysis ◽  
Chloride Ions ◽  
Monoclinic Space Group ◽  
Haloalkane Dehalogenase ◽  
Molecular Tagging ◽  
In The Wild ◽  
Bradyrhizobium Elkanii

Haloalkane dehalogenases are a very important class of microbial enzymes for environmental detoxification of halogenated pollutants, for biocatalysis, biosensing and molecular tagging. The double mutant (Ile44Leu + Gln102His) of the haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 (DbeAΔCl) was constructed to study the role of the second halide-binding site previously discovered in the wild-type structure. The variant is less active, less stable in the presence of chloride ions and exhibits significantly altered substrate specificity when compared with the DbeAwt. DbeAΔCl was crystallized using the sitting-drop vapour-diffusion procedure with further optimization by the random microseeding technique. The crystal structure of the DbeAΔCl has been determined and refined to the 1.4 Å resolution. The DbeAΔCl crystals belong to monoclinic space group C121. The DbeAΔCl molecular structure was characterized and compared with five known haloalkane dehalogenases selected from the Protein Data Bank.

Synthesis, binding and structure–affinity studies of new ligands for the microsomal anti-estrogen binding site (AEBS)

2000 ◽  
Vol 8 (8) ◽  
pp. 2007-2016 ◽  
Author(s):  
Marc Poirot ◽  
Philippe De Medina ◽  
Frederic Delarue ◽  
Jean-Jacques Perie ◽  
Alain Klaebe ◽  
...  
Keyword(s):  
Binding Site ◽  
Estrogen Binding

Chromatographic resolution of the type II estrogen binding site and a tyrosinase-like enzymatic activity from rat uterine nuclei

Steroids ◽  
1994 ◽  
Vol 59 (4) ◽  
pp. 282-287 ◽  
Author(s):  
Charles L. Densmore ◽  
Thomas H. Schauweker ◽  
Rebecca R. Gregory ◽  
Brett Webb ◽  
Elvia Garcia ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Binding Site ◽  
Type Ii ◽  
Chromatographic Resolution ◽  
Estrogen Binding

Type II estrogen binding site agonist:

Chirality ◽  
2003 ◽  
Vol 15 (8) ◽  
pp. 674-679 ◽  
Author(s):  
Lester Pretlow ◽  
Roy Williams ◽  
Mark Elliott
Keyword(s):  
Binding Site ◽  
Type Ii ◽  
Estrogen Binding
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