Three-Dimensional Models of Estrogen Receptor Ligand Binding Domain Complexes, Based on Related Crystal Structures and Mutational and Structure−Activity Relationship Data†

1998 ◽  
Vol 41 (11) ◽  
pp. 1803-1814 ◽  
Author(s):  
Jean-Marie Wurtz ◽  
Ursula Egner ◽  
Nikolaus Heinrich ◽  
Dino Moras ◽  
Anke Mueller-Fahrnow
Keyword(s):  
Estrogen Receptor ◽  
Ligand Binding ◽  
Crystal Structures ◽  
Three Dimensional ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Receptor Ligand ◽  
Structure Activity ◽  
Three Dimensional Models ◽  
Estrogen Receptor Ligand

Towards further Understanding the Structural Requirements of Combretastatin- like Chalcones as Inhibitors of Microtubule Polymerization

2020 ◽  
Vol 16 (2) ◽  
pp. 155-166
Author(s):  
Naveen Dhingra ◽  
Anand Kar ◽  
Rajesh Sharma
Keyword(s):  
Three Dimensional ◽  
3D Qsar ◽  
Docking Study ◽  
Structure Activity Relationship ◽  
Docking Studies ◽  
Activity Relationship ◽  
Structural Requirement ◽  
Ligand Interaction ◽  
Microtubule Polymerization ◽  
Structure Activity

Background: Microtubules are dynamic filamentous cytoskeletal structures which play several key roles in cell proliferation and trafficking. They are supposed to contribute in the development of important therapeutic targeting tumor cells. Chalcones are important group of natural compounds abundantly found in fruits & vegetables that are known to possess anticancer activity. We have used QSAR and docking studies to understand the structural requirement of chalcones for understanding the mechanism of microtubule polymerization inhibition. Methods: Three dimensional (3D) QSAR (CoMFA and CoMSIA), pharmacophore mapping and molecular docking studies were performed for the generation of structure activity relationship of combretastatin-like chalcones through statistical models and contour maps. Results: Structure activity relationship revealed that substitution of electrostatic, steric and donor groups may enhance the biological activity of compounds as inhibitors of microtubule polymerization. From the docking study, it was clear that compounds bind at the active site of tubulin protein. Conclusion: The given strategies of modelling could be an encouraging way for designing more potent compounds as well as for the elucidation of protein-ligand interaction.

Simulations of the Estrogen Receptor Ligand-Binding Domain:  Affinity of Natural Ligands and Xenoestrogens

2000 ◽  
Vol 43 (24) ◽  
pp. 4594-4605 ◽  
Author(s):  
B. Chris Oostenbrink ◽  
Jed W. Pitera ◽  
Marola M. H. van Lipzig ◽  
John H. N. Meerman ◽  
Wilfred F. van Gunsteren
Keyword(s):  
Estrogen Receptor ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Receptor Ligand ◽  
Natural Ligands ◽  
Estrogen Receptor Ligand
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