scholarly journals Recognition of LXXLL by Ligand Binding Domain of the Farnesoid X Receptor in Molecular Dynamics Simulation.

ChemInform ◽  
2007 ◽  
Vol 38 (9) ◽  
Author(s):  
Tao Zhang ◽  
Xi-Cheng Dong ◽  
Min-Bo Chen
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Farnesoid X Receptor ◽  
Dynamics Simulation

scholarly journals Asymmetric Structural Motions of the Homomeric α7 Nicotinic Receptor Ligand Binding Domain Revealed by Molecular Dynamics Simulation

2003 ◽  
Vol 85 (5) ◽  
pp. 3007-3018 ◽  
Author(s):  
Richard H. Henchman ◽  
Hai-Long Wang ◽  
Steven M. Sine ◽  
Palmer Taylor ◽  
J. Andrew McCammon
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Ligand Binding ◽  
Nicotinic Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Dynamics Simulation ◽  
Receptor Ligand

scholarly journals Ligand-binding regulation of LXR/RXR and LXR/PPAR heterodimerizations: SPR technology-based kinetic analysis correlated with molecular dynamics simulation

2005 ◽  
Vol 14 (3) ◽  
pp. 812-822 ◽  
Author(s):  
Liduo Yue ◽  
Fei Ye ◽  
Chunshan Gui ◽  
Haibin Luo ◽  
Jianhua Cai ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Ligand Binding ◽  
Kinetic Analysis ◽  
Dynamics Simulation

Zn2+ion of the snake venom metalloproteinase (SVMP) plays a critical role in ligand binding: a molecular dynamics simulation study

RSC Advances ◽  
2015 ◽  
Vol 5 (86) ◽  
pp. 70566-70576 ◽  
Author(s):  
Sathishkumar Chinnasamy ◽  
Selvaraman Nagamani ◽  
Karthikeyan Muthusamy
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Ligand Binding ◽  
Blood Coagulation ◽  
Snake Venom ◽  
Simulation Study ◽  
Tissue Damage ◽  
Critical Role ◽  
Dynamics Simulation ◽  
Snake Venom Metalloproteinase

Snake venom metalloproteinase (SVMP) is one of the major components of snake venom and it is a root causative agent for edema, local tissue damage, inflammation, blood coagulation and hemorrhage during the snake bite.

scholarly journals The nuclear bile acid receptor FXR is activated by PGC-1α in a ligand-dependent manner

2004 ◽  
Vol 382 (3) ◽  
pp. 913-921 ◽  
Author(s):  
Eiko KANAYA ◽  
Takuma SHIRAKI ◽  
Hisato JINGAMI
Keyword(s):  
Bile Acid ◽  
Ligand Binding ◽  
Transcriptional Activation ◽  
Expression System ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Farnesoid X Receptor ◽  
Dependent Manner ◽  
Acid Receptor ◽  
Bile Acid Receptor

The nuclear bile acid receptor FXR (farnesoid X receptor) is one of the key factors that suppress bile acid biosynthesis in the liver. PGC-1α [PPARγ (peroxisome-proliferator-activated receptor γ) co-activator-1α] is known to control energy homoeostasis in adipose tissue, skeletal muscle and liver. We performed cell-based reporter assays using the expression system of a GAL4–FXR chimaera, the ligand-binding domain of FXR fused to the DNA-binding domain of yeast GAL4, to find the co-activators for FXR. We found that the transcriptional activation of a reporter plasmid by a GAL4–FXR chimaera was strongly enhanced by PGC-1α, in a ligand-dependent manner. Transcriptional activation of the SHP (small heterodimer partner) gene by the FXR–RXRα (retinoid X receptor α) heterodimer was also enhanced by PGC-1α in the presence of CDCA (chenodeoxycholic acid). Co-immunoprecipitation and pull-down studies using glutathione S-transferase–PGC-1α fusion proteins revealed that the ligand-binding domain of FXR binds PGC-1α in a ligand-influenced manner both in vivo and in vitro. Furthermore, our studies revealed that SHP represses its own transcription, and the addition of excess amounts of PGC-1α can overcome the inhibitory effect of SHP. These observations indicate that PGC-1α mediates the ligand-dependent activation of FXR and transcription of SHP gene.

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