We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
AgonistPPARγ interactions: Molecular modeling study with docking approach.
- Authors
Xu, Xiao Ying; Cheng, Feng; Shen, Jian Hua; Luo, Xiao Min; Chen, Li Li; Yue, Li Duo; Du, Yi; Ye, Fei; Jiang, Shan Hao; Zhu, Da Yuan; Jiang, Hua Liang; Chen, Kai Xian
- Abstract
Docking simulation of 18 agonists with the ligand binding pocket (LBP) of PPARγ has been performed. The binding conformations and binding affinities of these agonists were obtained by use of the flexible docking protocol FlexX. Test compound calculations indicated that FlexX can reproduce the binding conformation of the crystal structure (root mean square deviation = 1.43 Å); moreover, the predicted binding affinities correlate well with the activities of these agonists. The interaction model and pharmacophore of PPARγ agonists were derived and the difference in biologic activities of these agonists can be well explained. The PPARγ agonists must have both polar head and the hydrophobic tail, which form hydrogen bonds and hydrophobic contacts with hydrophilic and hydrophobic regions of the LBP of PPARγ, respectively. In addition, a suitable linker is also necessary. © 2003 Wiley Periodicals, Inc. Int J Quantum Chem 93: 405410, 2003
- Publication
International Journal of Quantum Chemistry, 2003, Vol 93, Issue 6, p405
- ISSN
0020-7608
- Publication type
Article
- DOI
10.1002/qua.10575