scholarly journals Abscisic Acid Regulates Inflammation via Ligand-binding Domain-independent Activation of Peroxisome Proliferator-activated Receptor γ

2010 ◽  
Vol 286 (4) ◽  
pp. 2504-2516 ◽  
Author(s):  
Josep Bassaganya-Riera ◽  
Amir J. Guri ◽  
Pinyi Lu ◽  
Montse Climent ◽  
Adria Carbo ◽  
...  
Keyword(s):  
Abscisic Acid ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Domain Independent

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

scholarly journals Ajulemic Acid, a Synthetic Nonpsychoactive Cannabinoid Acid, Bound to the Ligand Binding Domain of the Human Peroxisome Proliferator-activated Receptor γ

2007 ◽  
Vol 282 (25) ◽  
pp. 18625-18633 ◽  
Author(s):  
Andre L. B. Ambrosio ◽  
Sandra M. G. Dias ◽  
Igor Polikarpov ◽  
Robert B. Zurier ◽  
Sumner H. Burstein ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Ajulemic Acid

scholarly journals Molecular Modeling of Quercetin Binding to the Peroxisome Proliferator-Activated Receptor-Gamma

2011 ◽  
Vol 68 (2) ◽  
Author(s):  
Cristina COMAN (ISVORANU) ◽  
Carmen SOCACIU
Keyword(s):  
Hydrogen Bond ◽  
Molecular Modeling ◽  
Ligand Binding ◽  
Binding Site ◽  
Binding Mode ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peroxisome Proliferator ◽  
Receptor Ligand ◽  
Peroxisome Proliferator Activated Receptor

The interaction between the quercetin (a generic flavonoid molecule) and the ligand binding domain of the peroxisome proliferator–activated receptor-gamma was investigated using the AutoDock software, which allows docking of molecular ligands to receptor macromolecules. AutoDock is able to find the most favourable binding site for quercetin on the receptor ligand binding domain and to predict the binding mode. The results show that the bonding is mainly driven through hydrogen bond type interactions and suggest the existence of two favourable quercetin conformations which coexist.

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