Faculty Opinions recommendation of Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor alpha (ERRalpha): crystal structure of ERRalpha ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1alpha.

2006 ◽  
Author(s):  
Fraydoon Rastinejad
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Transcriptional Activation ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Receptor Alpha ◽  
Estrogen Related Receptor

scholarly journals Docking of Phytochemicals to the Peroxisome Proliferator-Activated Receptor-Gamma Ligand Binding Domain

2012 ◽  
Vol 69 (2) ◽  
Author(s):  
Cristina COMAN ◽  
Carmen SOCACIU
Keyword(s):  
Hydrogen Bond ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peroxisome Proliferator ◽  
Amino Acid Residues ◽  
Theoretical Level ◽  
Hydrogen Atoms ◽  
Peroxisome Proliferator Activated Receptor ◽  
Hydrogen Bond Interactions

In this study, the interaction between the phytochemical molecules - piperine and pipernonaline - and the ligand binding domain of the peroxisome proliferator-activated receptor-γ is investigated at a theoretical level by using the AutoDock software, which is a program that allows docking of molecular ligands to receptor macromolecules. The docking results show that the ligandreceptor complexes are formed through hydrogen bond interactions. The hydrogen bonds involve oxygen atoms in the piperine and pipernonaline ligands as hydrogen bond acceptors and hydrogen atoms from =NH or -NH groups of the amino acid residues in the receptor as hydrogen bond donors.  2

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